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Information on EC 1.8.98.5 - H2:CoB-CoM heterodisulfide,ferredoxin reductase
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1.8.98.5 H2:CoB-CoM heterodisulfide,ferredoxin reductaseIUBMB Comments
This enzyme complex is found in H2-oxidizing CO2-reducing methanogenic archaea such as Methanothermobacter thermautotrophicus. It consists of a cytoplasmic complex of HdrABC reductase and MvhAGD hydrogenase. Electron pairs donated by the hydrogenase are transferred via its delta subunit to the HdrA subunit of the reductase, where they are bifurcated, reducing both ferredoxin and CoB-CoM heterodisulfide. The reductase can also form a similar complex with formate dehydrogenase, see EC 1.8.98.6, formate:CoB-CoM heterodisulfide,ferredoxin reductase. cf. EC 1.8.7.3, ferredoxin:CoB-CoM heterodisulfide reductase, EC 1.8.98.4, coenzyme F420:CoB-CoM heterodisulfide,ferredoxin reductase, and EC 1.8.98.1, dihydromethanophenazine:CoB-CoM heterodisulfide reductase.
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Word Map
- 1.8.98.5
- methanococcus
-
methanogenic
- hydrogenases
- archaea
- nickel
- epr
- voltae
- sulfur
- methanosarcina
-
energy-conserving
- ni
-
hyperfine
-
methanobacterium
- selenocysteine
-
f420-reducing
- fad
-
heterolytic
- methane
-
selenium-containing
- barkeri
- illumination
- selenium
- thermoautotrophicum
- com-s-s-cob
-
methanothermobacter
-
hydrogenotrophic
-
non-heme
- marburgensis
-
acid-labile
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
2
+
+
+
2
=
2
+
2
+
2
reduced ferredoxin [iron-sulfur] cluster
+
+
+
2
=
2
+
2
oxidized ferredoxin [iron-sulfur] cluster
+
Synonyms
f420-non-reducing hydrogenase, heterodisulfide reductase complex, hdrabc-mvhagd, mvhadg, mvhadg/hdrabc, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CoB-CoM heterodisulfide reductase
F420-non-reducing hydrogenase
H2-driven FBEB
H2: heterodisulfide oxidoreductase complex
HdrA
hdrA1B1C1
HdrABC
HdrABC-MvhAGD
HdrB
HdrC
HdrDE
HdrDE-VhoGAC
heterodisulfide reductase
heterodisulfide reductase complex
hydrogenase
Mvh
MvhA
MvhADG
MvhADG/HdrABC
MvhD
MvhG
VhoGAC
Vhu
additional information
CoB-CoM heterodisulfide reductase
-
CoB-CoM heterodisulfide reductase
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-
CoB-CoM heterodisulfide reductase
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-
CoB-CoM heterodisulfide reductase
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-
CoB-CoM heterodisulfide reductase
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-
CoB-CoM heterodisulfide reductase
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-
CoB-CoM heterodisulfide reductase
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-
CoB-CoM heterodisulfide reductase
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-
H2: heterodisulfide oxidoreductase complex
Methanobacterium thermoautotrophicus DSM 2133
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-
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HdrABC-MvhAGD
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HdrABC-MvhAGD
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-
HdrABC-MvhAGD
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-
HdrABC-MvhAGD
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-
HdrABC-MvhAGD
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-
HdrABC-MvhAGD
-
-
HdrABC-MvhAGD
-
-
HdrABC-MvhAGD
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reaction mechanism, overview
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reaction mechanism, overview
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
the two HdrA subunits form the interprotomer contact which implicates an electronic connection between the two FADs and two [4Fe-4S] clusters. The bifurcating FAD buried inside HdrA is the core of the complex from which three electron routes branch off. The single electrons from the [NiFe] center flow to the FAD from which a high-potential electron is transferred to the non-cubane (nc) [4Fe-4S] clusters and a low-potential electron to the Fd domain. FAD-binding site in HdrA with a isoalloxazine ring that is localized between two Rossmann fold domains, the two linkers between them and the adjacent HdrA partner. The most striking interaction is formed between N5 and the positively charged Lys409 that is kept at its position by interactions with Glu356, Lys187-O and a H2O multiply linked with the polypeptide. The electron transfer route is interrupted between the [2Fe-2S] cluster of MvhD and FAD
-
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
the two HdrA subunits form the interprotomer contact which implicates an electronic connection between the two FADs and two [4Fe-4S] clusters. The bifurcating FAD buried inside HdrA is the core of the complex from which three electron routes branch off. The single electrons from the [NiFe] center flow to the FAD from which a high-potential electron is transferred to the non-cubane (nc) [4Fe-4S] clusters and a low-potential electron to the Fd domain. FAD-binding site in HdrA with a isoalloxazine ring that is localized between two Rossmann fold domains, the two linkers between them and the adjacent HdrA partner. The most striking interaction is formed between N5 and the positively charged Lys409 that is kept at its position by interactions with Glu356, Lys187-O and a H2O multiply linked with the polypeptide. The electron transfer route is interrupted between the [2Fe-2S] cluster of MvhD and FAD
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
the two HdrA subunits form the interprotomer contact which implicates an electronic connection between the two FADs and two [4Fe-4S] clusters. The bifurcating FAD buried inside HdrA is the core of the complex from which three electron routes branch off. The single electrons from the [NiFe] center flow to the FAD from which a high-potential electron is transferred to the non-cubane (nc) [4Fe-4S] clusters and a low-potential electron to the Fd domain. FAD-binding site in HdrA with a isoalloxazine ring that is localized between two Rossmann fold domains, the two linkers between them and the adjacent HdrA partner. The most striking interaction is formed between N5 and the positively charged Lys409 that is kept at its position by interactions with Glu356, Lys187-O and a H2O multiply linked with the polypeptide. The electron transfer route is interrupted between the [2Fe-2S] cluster of MvhD and FAD
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reaction mechanism, overview
-
-
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
the two HdrA subunits form the interprotomer contact which implicates an electronic connection between the two FADs and two [4Fe-4S] clusters. The bifurcating FAD buried inside HdrA is the core of the complex from which three electron routes branch off. The single electrons from the [NiFe] center flow to the FAD from which a high-potential electron is transferred to the non-cubane (nc) [4Fe-4S] clusters and a low-potential electron to the Fd domain. FAD-binding site in HdrA with a isoalloxazine ring that is localized between two Rossmann fold domains, the two linkers between them and the adjacent HdrA partner. The most striking interaction is formed between N5 and the positively charged Lys409 that is kept at its position by interactions with Glu356, Lys187-O and a H2O multiply linked with the polypeptide. The electron transfer route is interrupted between the [2Fe-2S] cluster of MvhD and FAD
-
-
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reaction mechanism, overview
-
-
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
the two HdrA subunits form the interprotomer contact which implicates an electronic connection between the two FADs and two [4Fe-4S] clusters. The bifurcating FAD buried inside HdrA is the core of the complex from which three electron routes branch off. The single electrons from the [NiFe] center flow to the FAD from which a high-potential electron is transferred to the non-cubane (nc) [4Fe-4S] clusters and a low-potential electron to the Fd domain. FAD-binding site in HdrA with a isoalloxazine ring that is localized between two Rossmann fold domains, the two linkers between them and the adjacent HdrA partner. The most striking interaction is formed between N5 and the positively charged Lys409 that is kept at its position by interactions with Glu356, Lys187-O and a H2O multiply linked with the polypeptide. The electron transfer route is interrupted between the [2Fe-2S] cluster of MvhD and FAD
-
-
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reaction mechanism, overview
-
-
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
the two HdrA subunits form the interprotomer contact which implicates an electronic connection between the two FADs and two [4Fe-4S] clusters. The bifurcating FAD buried inside HdrA is the core of the complex from which three electron routes branch off. The single electrons from the [NiFe] center flow to the FAD from which a high-potential electron is transferred to the non-cubane (nc) [4Fe-4S] clusters and a low-potential electron to the Fd domain. FAD-binding site in HdrA with a isoalloxazine ring that is localized between two Rossmann fold domains, the two linkers between them and the adjacent HdrA partner. The most striking interaction is formed between N5 and the positively charged Lys409 that is kept at its position by interactions with Glu356, Lys187-O and a H2O multiply linked with the polypeptide. The electron transfer route is interrupted between the [2Fe-2S] cluster of MvhD and FAD
-
-
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reaction mechanism, overview
-
-
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reaction mechanism, overview
-
-
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
the two HdrA subunits form the interprotomer contact which implicates an electronic connection between the two FADs and two [4Fe-4S] clusters. The bifurcating FAD buried inside HdrA is the core of the complex from which three electron routes branch off. The single electrons from the [NiFe] center flow to the FAD from which a high-potential electron is transferred to the non-cubane (nc) [4Fe-4S] clusters and a low-potential electron to the Fd domain. FAD-binding site in HdrA with a isoalloxazine ring that is localized between two Rossmann fold domains, the two linkers between them and the adjacent HdrA partner. The most striking interaction is formed between N5 and the positively charged Lys409 that is kept at its position by interactions with Glu356, Lys187-O and a H2O multiply linked with the polypeptide. The electron transfer route is interrupted between the [2Fe-2S] cluster of MvhD and FAD
-
-
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reaction mechanism, overview
-
-
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
the two HdrA subunits form the interprotomer contact which implicates an electronic connection between the two FADs and two [4Fe-4S] clusters. The bifurcating FAD buried inside HdrA is the core of the complex from which three electron routes branch off. The single electrons from the [NiFe] center flow to the FAD from which a high-potential electron is transferred to the non-cubane (nc) [4Fe-4S] clusters and a low-potential electron to the Fd domain. FAD-binding site in HdrA with a isoalloxazine ring that is localized between two Rossmann fold domains, the two linkers between them and the adjacent HdrA partner. The most striking interaction is formed between N5 and the positively charged Lys409 that is kept at its position by interactions with Glu356, Lys187-O and a H2O multiply linked with the polypeptide. The electron transfer route is interrupted between the [2Fe-2S] cluster of MvhD and FAD
-
-
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reaction mechanism, overview
-
-
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ = 2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
the two HdrA subunits form the interprotomer contact which implicates an electronic connection between the two FADs and two [4Fe-4S] clusters. The bifurcating FAD buried inside HdrA is the core of the complex from which three electron routes branch off. The single electrons from the [NiFe] center flow to the FAD from which a high-potential electron is transferred to the non-cubane (nc) [4Fe-4S] clusters and a low-potential electron to the Fd domain. FAD-binding site in HdrA with a isoalloxazine ring that is localized between two Rossmann fold domains, the two linkers between them and the adjacent HdrA partner. The most striking interaction is formed between N5 and the positively charged Lys409 that is kept at its position by interactions with Glu356, Lys187-O and a H2O multiply linked with the polypeptide. The electron transfer route is interrupted between the [2Fe-2S] cluster of MvhD and FAD
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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-
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SYSTEMATIC NAME
IUBMB Comments
CoB,CoM,ferredoxin:H2 oxidoreductase
This enzyme complex is found in H2-oxidizing CO2-reducing methanogenic archaea such as Methanothermobacter thermautotrophicus. It consists of a cytoplasmic complex of HdrABC reductase and MvhAGD hydrogenase. Electron pairs donated by the hydrogenase are transferred via its delta subunit to the HdrA subunit of the reductase, where they are bifurcated, reducing both ferredoxin and CoB-CoM heterodisulfide. The reductase can also form a similar complex with formate dehydrogenase, see EC 1.8.98.6, formate:CoB-CoM heterodisulfide,ferredoxin reductase. cf. EC 1.8.7.3, ferredoxin:CoB-CoM heterodisulfide reductase, EC 1.8.98.4, coenzyme F420:CoB-CoM heterodisulfide,ferredoxin reductase, and EC 1.8.98.1, dihydromethanophenazine:CoB-CoM heterodisulfide reductase.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
coenzyme B-coenzyme M disulfide + ferredoxin + 2 H2
coenzyme B + coenzyme M + reduced ferredoxin2- + 2 H+
coenzyme B-coenzyme M disulfide + metronidazole + 2 H2
coenzyme B + coenzyme M + reduced metronidazole2- + 2 H+
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
in Escherichia coli recombinantly expressed Clostridium pasteurianum ferredoxin is used as cosubstrate. The Vdu containing complexes show higher activity with hydrogen compared to formate. H2 oxidation by FBEB by the MvhHdr complex reduces ferredoxin (Fd) to almost 100%
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-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
in Escherichia coli recombinantly expressed Clostridium pasteurianum ferredoxin is used as cosubstrate. The Vdu containing complexes show higher activity with hydrogen compared to formate. H2 oxidation by FBEB by the MvhHdr complex reduces ferredoxin (Fd) to almost 100%
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, and CoM-S-S-CoB is a high-potential acceptor
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, and CoM-S-S-CoB is a high-potential acceptor
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, and CoM-S-S-CoB is a high-potential acceptor
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, and CoM-S-S-CoB is a high-potential acceptor
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, and CoM-S-S-CoB is a high-potential acceptor
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, and CoM-S-S-CoB is a high-potential acceptor
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, and CoM-S-S-CoB is a high-potential acceptor
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, while CoM-S-S-CoB is a high-potential acceptor
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
H2 is a medium-potential donor, while ferredoxin is a low-potential acceptor, while CoM-S-S-CoB is a high-potential acceptor
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
electron flow occurs from hydrogen to CoM-S-S-CoB in the enzyme complex, while methanophenazine (MPhen) derivative is the potential electron carrier in the membranes of Methanonatronarchaeum thermophilum strain AMET1
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
electron flow occurs from hydrogen to CoM-S-S-CoB in the enzyme complex, while methanophenazine (MPhen) derivative is the potential electron carrier in the membranes of Methanonatronarchaeum thermophilum strain AMET1
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
Methanosarcina barkeri MS DSM 800
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
coenzyme B-coenzyme M disulfide + ferredoxin + 2 H2
coenzyme B + coenzyme M + reduced ferredoxin2- + 2 H+
HdrABC catalyzes the CoM-S-S-CoB-dependent reduction of ferredoxin with H2, coupling the endergonic reduction of ferredoxin to the exergonic reduction of coenzyme B-coenzyme M disulfide. Per mole CoM-S-S-CoB added, 1 mol of ferredoxin is reduced, indicating an electron bifurcation coupling mechanism. The stoichiometry of coupling is consistent with an ATP gain per mole methane from 4 H2 and CO2 of near 0.5
-
-
?
coenzyme B-coenzyme M disulfide + ferredoxin + 2 H2
coenzyme B + coenzyme M + reduced ferredoxin2- + 2 H+
HdrABC catalyzes the CoM-S-S-CoB-dependent reduction of ferredoxin with H2, coupling the endergonic reduction of ferredoxin to the exergonic reduction of coenzyme B-coenzyme M disulfide. Per mole CoM-S-S-CoB added, 1 mol of ferredoxin is reduced, indicating an electron bifurcation coupling mechanism. The stoichiometry of coupling is consistent with an ATP gain per mole methane from 4 H2 and CO2 of near 0.5
-
-
?
coenzyme B-coenzyme M disulfide + metronidazole + 2 H2
coenzyme B + coenzyme M + reduced metronidazole2- + 2 H+
purified complex shows a twofold higher specific activity with ferredoxin than with metronidazole
-
-
?
coenzyme B-coenzyme M disulfide + metronidazole + 2 H2
coenzyme B + coenzyme M + reduced metronidazole2- + 2 H+
purified complex shows a twofold higher specific activity with ferredoxin than with metronidazole
-
-
?
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
Methanobacterium thermoautotrophicus
-
-
-
-
?
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
Methanobacterium thermoautotrophicus DSM 2133
-
-
-
-
?
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
-
-
-
-
?
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
-
-
-
-
?
H2 + oxidized methyl viologen + CoM-S-S-CoB
reduced methyl viologen + CoB + CoM + H+
Methanobacterium thermoautotrophicus
-
-
-
-
?
H2 + oxidized methyl viologen + CoM-S-S-CoB
reduced methyl viologen + CoB + CoM + H+
Methanobacterium thermoautotrophicus DSM 2133
-
-
-
-
?
H2 + oxidized methyl viologen + CoM-S-S-CoB
reduced methyl viologen + CoB + CoM + H+
-
-
-
-
?
H2 + oxidized methyl viologen + CoM-S-S-CoB
reduced methyl viologen + CoB + CoM + H+
-
-
-
-
?
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
reduced metronidazole + CoB + CoM + H+
H2 + oxidized metronidazole + CoM-S-S-CoB
-
-
-
-
?
reduced metronidazole + CoB + CoM + H+
H2 + oxidized metronidazole + CoM-S-S-CoB
-
-
-
-
?
additional information
?
-
Methanobacterium thermoautotrophicus
-
no activity with coenzyme F420
-
-
?
additional information
?
-
Methanobacterium thermoautotrophicus DSM 2133
-
no activity with coenzyme F420
-
-
?
additional information
?
-
heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
-
-
-
additional information
?
-
-
the non-FBEB reduction of Fd by Vhu (H2 oxidation) or Fdh (formate oxidation) is not kinetically dominant
-
-
-
additional information
?
-
-
the non-FBEB reduction of Fd by Vhu (H2 oxidation) or Fdh (formate oxidation) is not kinetically dominant
-
-
-
additional information
?
-
heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
-
-
-
additional information
?
-
-
heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
-
-
-
additional information
?
-
heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
-
-
-
additional information
?
-
heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
-
-
-
additional information
?
-
heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
-
-
-
additional information
?
-
heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
-
-
-
additional information
?
-
heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
-
-
-
additional information
?
-
heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
-
-
-
additional information
?
-
heterodisulfide reductase (HdrABC) reduces the disulfide bond with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. The exergonic reduction of CoMS-SCoB drives the endergonic reduction of CO2 in the first step via FBEB by HdrABC
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
-
?
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
Methanosarcina barkeri MS DSM 800
-
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
2 H2 + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
Methanobacterium thermoautotrophicus
-
-
-
-
?
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
Methanobacterium thermoautotrophicus DSM 2133
-
-
-
-
?
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
-
-
-
-
?
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
-
-
-
-
?
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
H2 + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
electron-bifurcating FAD in HdrA
FAD
electron-bifurcating FAD in HdrA
FAD
-
the bifurcating FAD of HdrA sequentially accepts two electrons from the [2Fe-2S] cluster that contrasts with other characterized FBEB enzymes for which a hydride is donated to FAD
Fe-S center
-
two [4Fe-4S] clusters of the inserted ferredoxin (Fd) domain
Fe-S center
-
[4Fe-4S] clusters. Standard HdrC-like components consist of a Fd-like domain. It can be regarded as a linker module that electronically wires HdrA to HdrB by its two [4Fe-4S] clusters. HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs
Fe-S center
[4Fe-4S] clusters. Standard HdrC-like components consist of a Fd-like domain. It can be regarded as a linker module that electronically wires HdrA to HdrB by its two [4Fe-4S] clusters. HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs
Fe-S center
[4Fe-4S] clusters. Standard HdrC-like components consist of a Fd-like domain. It can be regarded as a linker module that electronically wires HdrA to HdrB by its two [4Fe-4S] clusters. HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs
Ferredoxin
-
standard HdrC-like components consist of a Fd-like domain
-
Ferredoxin
standard HdrC-like components consist of a Fd-like domain
-
Ferredoxin
standard HdrC-like components consist of a Fd-like domain. The TrxR domain is flanked by attached N- and C-terminal domains and an inserted Fd domain hosting one, two and again two [4Fe-4S] clusters, respectively. The low-potential acceptor Fd was not found in the complex, but electron transfer to it most possibly involves the [4Fe-4S] cluster of the Fd domain in HdrA
-
additional information
a methanophenazine-like cofactor functions as an electron carrier between the hydrogenase/formate dehydrogenase and the heterodisulfide reductase, cf. EC 1.8.98.1
-
additional information
-
MvhD, the component was originally referred to as subunit of the hydrogenase component (Mvh, methyl viologen-dependent hydrogenase) in the archetypical MvhAGD-HdrABC complex. MvhD-like components may be involved in the assumed switch from one-electron to two-electron transfer. They may be dispensable, when direct hydride donors such as NAD(P)H or F420H2 directly reduce the electron-bifurcating flavin, although not in the H2:CoB-CoM heterodisulfide,ferredoxin reductase function
-
additional information
MvhD, the component was originally referred to as subunit of the hydrogenase component (Mvh, methyl viologen-dependent hydrogenase) in the archetypical MvhAGD-HdrABC complex. MvhD-like components may be involved in the assumed switch from one-electron to two-electron transfer. They may be dispensable, when direct hydride donors such as NAD(P)H or F420H2 directly reduce the electron-bifurcating flavin, although not in the H2:CoB-CoM heterodisulfide,ferredoxin reductase function
-
additional information
MvhD, the component was originally referred to as subunit of the hydrogenase component (Mvh, methyl viologen-dependent hydrogenase) in the archetypical MvhAGD-HdrABC complex. MvhD-like components may be involved in the assumed switch from one-electron to two-electron transfer. They may be dispensable, when direct hydride donors such as NAD(P)H or F420H2 directly reduce the electron-bifurcating flavin, although not in the H2:CoB-CoM heterodisulfide,ferredoxin reductase function
-
additional information
the FAD binding site is encapsulated from bulk solvent preventing binding of hydride donors such as NADH or F420H2. The high-potential branch from FAD to the active-site non-cubane [4Fe-4S] clusters in HdrB proceeds via [4Fe-4S] clusters bound to the HdrBC subunits. The non-cubane clusters can be described as fused [3Fe-4S]/[2Fe-2S] subclusters, sharing one iron and one sulfur
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Methanobacterium thermoautotrophicus
-
the enzyme contains approximately 26 mol non-heme iron
KCl
activates HdrDE activity, best at 3 M KCl, about 50% activity at 2 and 4 M KCl
NaCl
activates VhoGAC activity, highest activity at 1 M
additional information
at pH 7.5, the specific activity of HdrDE with 2 M potassium chloride is about 40% higher than with 2 M sodium chloride
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the FBEB specific activity is slightly reduced when 1.6 M phosphate is replaced with 1.5 M phosphate buffer and 100 mM MOPS, although a similar activity is observed in 1.5 M ammonium sulfate and 100 mM MOPS. The FBEB specific activity is significantly reduced in 1.6 M MOPS
-
additional information
no inhibition of HdrDE and VhoGAC by diphenyleneiodonium chloride
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
high concentrations of phosphate buffer are required for optimal FBEB activities in vitro, which because they promote hydrophobic protein-protein interactions between the inserted ferredoxin domain on HdrA and Fd
-
CoM-S-S-CoB disulfide
reduction of CO2 by H2 is greatly stimulated by the CoM-S-S-CoB disulfide
-
CoM-S-S-CoB disulfide
-
reduction of CO2 by H2 is greatly stimulated by the CoM-S-S-CoB disulfide
-
CoM-S-S-CoB disulfide
reduction of CO2 by H2 is greatly stimulated by the CoM-S-S-CoB disulfide
-
potassium phosphate
complex is most active in presence of 1.6 M potassium phosphate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10.7
CoM-S-S-CoB reduction with methyl viologen as artificial electron donor by HdrDE, membrane fraction, pH 7.5, temperature not specified in the publication, at 2 M KCl
110
HdrABC complex with 100% H2 in the gas phase, pH 7.6, 60°C
20.1
VhoGAC activity on H2 with methyl viologen as artificial electron acceptor, membrane fraction, pH 9.5, temperature not specified in the publication, at 2 M NaCl
3.4
CoM-S-S-CoB reduction with methyl viologen as artificial electron donor by HdrDE, membrane fraction, pH 8.5, temperature not specified in the publication, at 2 M KCl
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 10.5
enzyme activity range, profile overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CoB-CoM heterodisulfide reductase subunit E; isolated from a hypersaline soda lake
UniProt
brenda
CoB-CoM heterodisulfide reductase subunit E; isolated from a hypersaline soda lake
UniProt
brenda
and strains Mm1264 and Mm1265, derivatives of strain S2 incorporating a polyHis-tag at the C-terminus of HdrB (1264) and at the C-terminus of FdhA (1265), respectively
-
-
brenda
CoB-CoM heterodisulfide reductase iron-sulfur subunits A, B1, B2, C1, and C2
UniProt
brenda
and strains Mm1264 and Mm1265, derivatives of strain S2 incorporating a polyHis-tag at the C-terminus of HdrB (1264) and at the C-terminus of FdhA (1265), respectively
-
-
brenda
CoB-CoM heterodisulfide reductase iron-sulfur subunits A, B1, B2, C1, and C2
UniProt
brenda
CoB-CoM heterodisulfide reductase iron-sulfur subunits A, B, and C; Methanobacterium thermoautotrophicum
UniProt
brenda
genes encoding subunits HdrA, HdrB, HdrC, MvhA, MvhG, and MvhD; Methanobacterium thermoautotrophicum
UniProt
brenda
CoB-CoM heterodisulfide reductase iron-sulfur subunits A, B, and C; Methanobacterium thermoautotrophicum
UniProt
brenda
genes encoding subunits HdrA, HdrB, HdrC, MvhA, MvhG, and MvhD; Methanobacterium thermoautotrophicum
UniProt
brenda
CoB-CoM heterodisulfide reductase iron-sulfur subunits A, B, and C; Methanobacterium thermoautotrophicum
UniProt
brenda
genes encoding subunits HdrA, HdrB, HdrC, MvhA, MvhG, and MvhD; Methanobacterium thermoautotrophicum
UniProt
brenda
CoB-CoM heterodisulfide reductase iron-sulfur subunits A, B, and C; Methanobacterium thermoautotrophicum
UniProt
brenda
genes encoding subunits HdrA, HdrB, HdrC, MvhA, MvhG, and MvhD; Methanobacterium thermoautotrophicum
UniProt
brenda
CoB-CoM heterodisulfide reductase iron-sulfur subunits A, B, and C; Methanobacterium thermoautotrophicum
UniProt
brenda
genes encoding subunits HdrA, HdrB, HdrC, MvhA, MvhG, and MvhD; Methanobacterium thermoautotrophicum
UniProt
brenda
CoB-CoM heterodisulfide reductase iron-sulfur subunits A, B, and C; Methanobacterium thermoautotrophicum
UniProt
brenda
genes encoding subunits HdrA, HdrB, HdrC, MvhA, MvhG, and MvhD; Methanobacterium thermoautotrophicum
UniProt
brenda
CoB-CoM heterodisulfide reductase iron-sulfur subunits A, B, and C; Methanobacterium thermoautotrophicum
UniProt
brenda
genes encoding subunits HdrA, HdrB, HdrC, MvhA, MvhG, and MvhD; Methanobacterium thermoautotrophicum
UniProt
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genes encoding subunits HdrA, HdrB, HdrC, MvhA, MvhG, and MvhD
UniProt
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Methanonatronarchaeum thermophilum strain AMET1 is able to grow on all tested substrates (methanol, trimethylamine (TMA), dimethylamine (DMA), monomethylamine (MMA)) in combination with formate or molecular hydrogen
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Methanonatronarchaeum thermophilum strain AMET1 is able to grow on all tested substrates (methanol, trimethylamine (TMA), dimethylamine (DMA), monomethylamine (MMA)) in combination with formate or molecular hydrogen
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coculture of Methanosarcina barkeri with Pelobacter carbinolicus, transcriptome analysis, overview. Out of the 3809 predicted protein-coding genes in the Methanosarcina barkeri MS genome, 1912 and 1909 genes have expression levels that are higher than the median in HIT-grown cells, respectively
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coculture of Methanosarcina barkeri with Pelobacter carbinolicus, transcriptome analysis, overview. Out of the 3809 predicted protein-coding genes in the Methanosarcina barkeri MS genome, 1912 and 1909 genes have expression levels that are higher than the median in HIT-grown cells, respectively
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coculture of Methanosarcina barkeri with Pelobacter carbinolicus, transcriptome analysis, overview. Out of the 3809 predicted protein-coding genes in the Methanosarcina barkeri MS genome, 1912 and 1909 genes have expression levels that are higher than the median in HIT-grown cells, respectively
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Methanosarcina barkeri MS DSM 800
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coculture of Methanosarcina barkeri with Pelobacter carbinolicus, transcriptome analysis, overview. Out of the 3809 predicted protein-coding genes in the Methanosarcina barkeri MS genome, 1912 and 1909 genes have expression levels that are higher than the median in HIT-grown cells, respectively
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the catalytic subunit of heterodisulfide reductase (HdrD) is located at the cytoplasmic side of the cytoplasmic membrane. The oxidation of H2 takes place via a membrane-bound hydrogenase (VhoGAC)
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the catalytic subunit of heterodisulfide reductase (HdrD) is located at the cytoplasmic side of the cytoplasmic membrane. The oxidation of H2 takes place via a membrane-bound hydrogenase (VhoGAC)
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
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general architecture and occurrence of HdrA(BC)-containing complexes, overview. Overview of some biochemically and/or genetically studied HdrA(BC)-containing enzyme complexes. HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs. This cysteine-rich binding motif is invariant in all HdrB components of methanogens, but also conserved in bacterial HdrB-like components where only in some cases cysteines may be substituted by serines and an aspartate. This conservation indicates that disulfide intermediates other than the CoM-S-S-CoB heterodisulfide, e.g. formed by proteinogenic cysteine residues, may also be involved in catalysis of HdrA(BC) enzymes from non-methanogens. They may transfer electrons further to an additional oxidoreductase module. The MvhD component was originally referred to as subunit of the hydrogenase component (Mvh, methyl viologen-dependent hydrogenase) in the archetypical MvhAGD-HdrABC complex. MvhD-like components may be involved in the assumed switch from one-electron to two-electron transfer. They may be dispensable, when direct hydride donors such as NAD(P)H or F420H2 directly reduce the electron-bifurcating flavin, although not in the H2:CoB-CoM heterodisulfide,ferredoxin reductase function
evolution
general architecture and occurrence of HdrA(BC)-containing complexes, overview. Overview of some biochemically and/or genetically studied HdrA(BC)-containing enzyme complexes. HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs. This cysteine-rich binding motif is invariant in all HdrB components of methanogens, but also conserved in bacterial HdrB-like components where only in some cases cysteines may be substituted by serines and an aspartate. This conservation indicates that disulfide intermediates other than the CoM-S-S-CoB heterodisulfide, e.g. formed by proteinogenic cysteine residues, may also be involved in catalysis of HdrA(BC) enzymes from non-methanogens. They may transfer electrons further to an additional oxidoreductase module. The MvhD component was originally referred to as subunit of the hydrogenase component (Mvh, methyl viologen-dependent hydrogenase) in the archetypical MvhAGD-HdrABC complex. MvhD-like components may be involved in the assumed switch from one-electron to two-electron transfer. They may be dispensable, when direct hydride donors such as NAD(P)H or F420H2 directly reduce the electron-bifurcating flavin, although not in the H2:CoB-CoM heterodisulfide,ferredoxin reductase function
evolution
general architecture and occurrence of HdrA(BC)-containing complexes, X-ray structure of the MvhAGD-HdrABC complex of Methanothermococcus thermolithotrophicus, overview. Overview of some biochemically and/or genetically studied HdrA(BC)-containing enzyme complexes. HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs. This cysteine-rich binding motif is invariant in all HdrB components of methanogens, but also conserved in bacterial HdrB-like components where only in some cases cysteines may be substituted by serines and an aspartate. This conservation indicates that disulfide intermediates other than the CoM-S-S-CoB heterodisulfide, e.g. formed by proteinogenic cysteine residues, may also be involved in catalysis of HdrA(BC) enzymes from non-methanogens. They may transfer electrons further to an additional oxidoreductase module. The MvhD component was originally referred to as subunit of the hydrogenase component (Mvh, methyl viologen-dependent hydrogenase) in the archetypical MvhAGD-HdrABC complex. MvhD-like components may be involved in the assumed switch from one-electron to two-electron transfer. They may be dispensable, when direct hydride donors such as NAD(P)H or F420H2 directly reduce the electron-bifurcating flavin, although not in the H2:CoB-CoM heterodisulfide,ferredoxin reductase function
evolution
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general architecture and occurrence of HdrA(BC)-containing complexes, overview. Overview of some biochemically and/or genetically studied HdrA(BC)-containing enzyme complexes. HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs. This cysteine-rich binding motif is invariant in all HdrB components of methanogens, but also conserved in bacterial HdrB-like components where only in some cases cysteines may be substituted by serines and an aspartate. This conservation indicates that disulfide intermediates other than the CoM-S-S-CoB heterodisulfide, e.g. formed by proteinogenic cysteine residues, may also be involved in catalysis of HdrA(BC) enzymes from non-methanogens. They may transfer electrons further to an additional oxidoreductase module. The MvhD component was originally referred to as subunit of the hydrogenase component (Mvh, methyl viologen-dependent hydrogenase) in the archetypical MvhAGD-HdrABC complex. MvhD-like components may be involved in the assumed switch from one-electron to two-electron transfer. They may be dispensable, when direct hydride donors such as NAD(P)H or F420H2 directly reduce the electron-bifurcating flavin, although not in the H2:CoB-CoM heterodisulfide,ferredoxin reductase function
-
evolution
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general architecture and occurrence of HdrA(BC)-containing complexes, overview. Overview of some biochemically and/or genetically studied HdrA(BC)-containing enzyme complexes. HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs. This cysteine-rich binding motif is invariant in all HdrB components of methanogens, but also conserved in bacterial HdrB-like components where only in some cases cysteines may be substituted by serines and an aspartate. This conservation indicates that disulfide intermediates other than the CoM-S-S-CoB heterodisulfide, e.g. formed by proteinogenic cysteine residues, may also be involved in catalysis of HdrA(BC) enzymes from non-methanogens. They may transfer electrons further to an additional oxidoreductase module. The MvhD component was originally referred to as subunit of the hydrogenase component (Mvh, methyl viologen-dependent hydrogenase) in the archetypical MvhAGD-HdrABC complex. MvhD-like components may be involved in the assumed switch from one-electron to two-electron transfer. They may be dispensable, when direct hydride donors such as NAD(P)H or F420H2 directly reduce the electron-bifurcating flavin, although not in the H2:CoB-CoM heterodisulfide,ferredoxin reductase function
-
evolution
-
general architecture and occurrence of HdrA(BC)-containing complexes, overview. Overview of some biochemically and/or genetically studied HdrA(BC)-containing enzyme complexes. HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs. This cysteine-rich binding motif is invariant in all HdrB components of methanogens, but also conserved in bacterial HdrB-like components where only in some cases cysteines may be substituted by serines and an aspartate. This conservation indicates that disulfide intermediates other than the CoM-S-S-CoB heterodisulfide, e.g. formed by proteinogenic cysteine residues, may also be involved in catalysis of HdrA(BC) enzymes from non-methanogens. They may transfer electrons further to an additional oxidoreductase module. The MvhD component was originally referred to as subunit of the hydrogenase component (Mvh, methyl viologen-dependent hydrogenase) in the archetypical MvhAGD-HdrABC complex. MvhD-like components may be involved in the assumed switch from one-electron to two-electron transfer. They may be dispensable, when direct hydride donors such as NAD(P)H or F420H2 directly reduce the electron-bifurcating flavin, although not in the H2:CoB-CoM heterodisulfide,ferredoxin reductase function
-
evolution
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general architecture and occurrence of HdrA(BC)-containing complexes, overview. Overview of some biochemically and/or genetically studied HdrA(BC)-containing enzyme complexes. HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs. This cysteine-rich binding motif is invariant in all HdrB components of methanogens, but also conserved in bacterial HdrB-like components where only in some cases cysteines may be substituted by serines and an aspartate. This conservation indicates that disulfide intermediates other than the CoM-S-S-CoB heterodisulfide, e.g. formed by proteinogenic cysteine residues, may also be involved in catalysis of HdrA(BC) enzymes from non-methanogens. They may transfer electrons further to an additional oxidoreductase module. The MvhD component was originally referred to as subunit of the hydrogenase component (Mvh, methyl viologen-dependent hydrogenase) in the archetypical MvhAGD-HdrABC complex. MvhD-like components may be involved in the assumed switch from one-electron to two-electron transfer. They may be dispensable, when direct hydride donors such as NAD(P)H or F420H2 directly reduce the electron-bifurcating flavin, although not in the H2:CoB-CoM heterodisulfide,ferredoxin reductase function
-
evolution
-
general architecture and occurrence of HdrA(BC)-containing complexes, overview. Overview of some biochemically and/or genetically studied HdrA(BC)-containing enzyme complexes. HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs. This cysteine-rich binding motif is invariant in all HdrB components of methanogens, but also conserved in bacterial HdrB-like components where only in some cases cysteines may be substituted by serines and an aspartate. This conservation indicates that disulfide intermediates other than the CoM-S-S-CoB heterodisulfide, e.g. formed by proteinogenic cysteine residues, may also be involved in catalysis of HdrA(BC) enzymes from non-methanogens. They may transfer electrons further to an additional oxidoreductase module. The MvhD component was originally referred to as subunit of the hydrogenase component (Mvh, methyl viologen-dependent hydrogenase) in the archetypical MvhAGD-HdrABC complex. MvhD-like components may be involved in the assumed switch from one-electron to two-electron transfer. They may be dispensable, when direct hydride donors such as NAD(P)H or F420H2 directly reduce the electron-bifurcating flavin, although not in the H2:CoB-CoM heterodisulfide,ferredoxin reductase function
-
evolution
-
general architecture and occurrence of HdrA(BC)-containing complexes, overview. Overview of some biochemically and/or genetically studied HdrA(BC)-containing enzyme complexes. HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs. This cysteine-rich binding motif is invariant in all HdrB components of methanogens, but also conserved in bacterial HdrB-like components where only in some cases cysteines may be substituted by serines and an aspartate. This conservation indicates that disulfide intermediates other than the CoM-S-S-CoB heterodisulfide, e.g. formed by proteinogenic cysteine residues, may also be involved in catalysis of HdrA(BC) enzymes from non-methanogens. They may transfer electrons further to an additional oxidoreductase module. The MvhD component was originally referred to as subunit of the hydrogenase component (Mvh, methyl viologen-dependent hydrogenase) in the archetypical MvhAGD-HdrABC complex. MvhD-like components may be involved in the assumed switch from one-electron to two-electron transfer. They may be dispensable, when direct hydride donors such as NAD(P)H or F420H2 directly reduce the electron-bifurcating flavin, although not in the H2:CoB-CoM heterodisulfide,ferredoxin reductase function
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metabolism
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generalized model for electron and proton flux during hydrogen interspecies electron transfer (HIT) and direct interspecies electron transfer (DIET) with growth on ethanol as an example, overview. H2 diffusion shuttles both electrons and protons between cells and carries both electrons and protons into the cell when cytoplasmic electron acceptors are reduced. The transcriptome reflects faster growth during HIT and possible greater importance of membrane and outer-surface proteins during DIET, but no specific upregulation of hydrogenase genes in response to growth via HIT
metabolism
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heterodisulfide reductase plays a central role in the methanogenesis cycle of Methanococcus maripaludis
metabolism
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in methanogens without cytochromes, the initial endergonic reduction of CO2 to formylmethanofuran with H2-derived electrons is coupled to the exergonic reduction of a heterodisulfide of coenzymes B and M by flavin-based electron bifurcation (FBEB). Methanococcus maripaludis employs three functional heterodisulfide reductase complexes for FBEB using hydrogen and formate. In Methanococcus maripaludis, FBEB is performed by a heterodisulfide reductase (Hdr) enzyme complex that involves hydrogenase (Vhu), although formate dehydrogenase (Fdh) has been proposed as an alternative to Vhu
metabolism
reduction of the disulfide of coenzyme M and coenzyme B (CoMS-SCoB) by heterodisulfide reductases (HdrED and HdrABC) is the final step in all methanogenic pathways. Flavin-based electron bifurcation (FBEB) by soluble HdrABC homologues play additional roles in driving essential endergonic reactions at the expense of the exergonic reduction of CoMS-SCoM. In the first step of the CO2 reduction pathway, HdrABC complexed with hydrogenase (EC 1.12.1.2) or formate dehydrogenase generates reduces ferredoxin (Fdx2-) for the endergonic reduction of CO2 coupled to the exergonic reduction of CoMS-SCoB dependent on FBEB of electrons from H2 or formate, respectively. Roles for HdrABC:hydrogenase complexes are also proposed for pathways wherein the methyl group of methanol is reduced to methane with electrons from H2. The HdrABC complexes catalyze FBEB-dependent oxidation of H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB. The Fdx2- supplies electrons for reduction of the methyl group to methane. In H2- independent pathways, threefourths of the methyl groups are oxidized producing Fdx2- and reduced coenzyme F420 (F420H2). The F420H2 donates electrons for reduction of the remaining methyl groups to methane requiring transfer of electrons from Fdx2- to F420. HdrA1B1C1 is proposed to catalyze FBEB-dependent oxidation of Fdx2- for the endergonic reduction of F420 driven by the exergonic reduction of CoMS-SCoB, see for EC 1.8.98.4. In H2- independent acetotrophic pathways (EC 1.8.98.5), the methyl group of acetate is reduced to methane with electrons derived from oxidation of the carbonyl group mediated by Fdx. Electron transport involves a membrane-bound complex (Rnf) that oxidizes Fdx2- and generates a NaC gradient driving ATP synthesis. It is postulated that F420 is reduced by Rnf requiring HdrA2B2C2 catalyzing FBEB-dependent oxidation of F420H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB (EC 1.8.98.4). The Fdx2- is recycled by Rnf and HdrA2B2C2 thereby conserving energy. The HdrA2B2C2 is also proposed to play a role in Fe(III)-dependent reverse methanogenesis. A flavin-based electron confurcating (FBEC) HdrABC complex is proposed for nitrate-dependent reverse methanogenesis in which the oxidation of CoM-SH/CoB-SH and Fdx2- is coupled to reduction of F420. The F420H2 donates electrons to a membrane complex that generates a proton gradient driving ATP synthesis
metabolism
reduction of the disulfide of coenzyme M and coenzyme B (CoMS-SCoB) by heterodisulfide reductases (HdrED and HdrABC) is the final step in all methanogenic pathways. Flavin-based electron bifurcation (FBEB) by soluble HdrABC homologues play additional roles in driving essential endergonic reactions at the expense of the exergonic reduction of CoMS-SCoM. In the first step of the CO2 reduction pathway, HdrABC complexed with hydrogenase (EC 1.12.1.2) or formate dehydrogenase generates reduces ferredoxin (Fdx2-) for the endergonic reduction of CO2 coupled to the exergonic reduction of CoMS-SCoB dependent on FBEB of electrons from H2 or formate, respectively. Roles for HdrABC:hydrogenase complexes are also proposed for pathways wherein the methyl group of methanol is reduced to methane with electrons from H2. The HdrABC complexes catalyze FBEB-dependent oxidation of H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB. The Fdx2- supplies electrons for reduction of the methyl group to methane. In H2- independent pathways, threefourths of the methyl groups are oxidized producing Fdx2- and reduced coenzyme F420 (F420H2). The F420H2 donates electrons for reduction of the remaining methyl groups to methane requiring transfer of electrons from Fdx2- to F420. HdrA1B1C1 is proposed to catalyze FBEB-dependent oxidation of Fdx2- for the endergonic reduction of F420 driven by the exergonic reduction of CoMS-SCoB, see for EC 1.8.98.4. In H2- independent acetotrophic pathways (EC 1.8.98.5), the methyl group of acetate is reduced to methane with electrons derived from oxidation of the carbonyl group mediated by Fdx. Electron transport involves a membrane-bound complex (Rnf) that oxidizes Fdx2- and generates a NaC gradient driving ATP synthesis. It is postulated that F420 is reduced by Rnf requiring HdrA2B2C2 catalyzing FBEB-dependent oxidation of F420H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB (EC 1.8.98.4). The Fdx2- is recycled by Rnf and HdrA2B2C2 thereby conserving energy. The HdrA2B2C2 is also proposed to play a role in Fe(III)-dependent reverse methanogenesis. A flavin-based electron confurcating (FBEC) HdrABC complex is proposed for nitrate-dependent reverse methanogenesis in which the oxidation of CoM-SH/CoB-SH and Fdx2- is coupled to reduction of F420. The F420H2 donates electrons to a membrane complex that generates a proton gradient driving ATP synthesis
metabolism
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reduction of the disulfide of coenzyme M and coenzyme B (CoMS-SCoB) by heterodisulfide reductases (HdrED and HdrABC) is the final step in all methanogenic pathways. Flavin-based electron bifurcation (FBEB) by soluble HdrABC homologues play additional roles in driving essential endergonic reactions at the expense of the exergonic reduction of CoMS-SCoM. In the first step of the CO2 reduction pathway, HdrABC complexed with hydrogenase or formate dehydrogenase generates reduced ferredoxin (Fdx2-) for the endergonic reduction of CO2 coupled to the exergonic reduction of CoMS-SCoB dependent on FBEB of electrons from H2 or formate. Roles for HdrABC:hydrogenase complexes are also proposed for pathways wherein the methyl group of methanol is reduced to methane with electrons from H2. The HdrABC complexes catalyze FBEB-dependent oxidation of H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB. The Fdx2- supplies electrons for reduction of the methyl group to methane. In H2- independent pathways, three-fourths of the methyl groups are oxidized producing Fdx2- and reduced coenzyme F420 (F420H2). The F420H2 donates electrons for reduction of the remaining methyl groups to methane requiring transfer of electrons from Fdx2- to F420. HdrA1B1C1 is proposed to catalyze FBEB-dependent oxidation of Fdx2- for the endergonic reduction of F420 driven by the exergonic reduction of CoMS-SCoB. F420 is reduced by Rnf requiring HdrA2B2C2 catalyzing FBEB-dependent oxidation of F420H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB. The Fdx2- is recycled by Rnf and HdrA2B2C2 thereby conserving energy. The HdrA2B2C2 is also proposed to play a role in Fe(III)-dependent reverse methanogenesis. A flavin-based electron confurcating (FBEC) HdrABC complex is proposed for nitrate-dependent reverse methanogenesis in which the oxidation of CoM-SH/CoB-SH and Fdx2- is coupled to reduction of F420. The F420H2 donates electrons to a membrane complex that generates a proton gradient driving ATP synthesis. Heterodisulfide reductase (HdrABC) reduces the disulfide bond in CoMS-SCoB with electrons supplied from the oxidation of 2H2 or 2HCO2H catalyzed by F420-independent hydrogenase or Fdh. Proposed role of FBEC by HdrA1B1C1 in methylotrophic pathways of methanogenesis, overview
metabolism
reduction of the disulfide of coenzyme M and coenzyme B (CoMS-SCoB) by heterodisulfide reductases (HdrED and HdrABC) is the final step in all methanogenic pathways. Flavin-based electron bifurcation (FBEB) by soluble HdrABC homologues play additional roles in driving essential endergonic reactions at the expense of the exergonic reduction of CoMS-SCoM. In the first step of the CO2 reduction pathway, HdrABC complexed with hydrogenase or formate dehydrogenase generates reduced ferredoxin (Fdx2-) for the endergonic reduction of CO2 coupled to the exergonic reduction of CoMS-SCoB dependent on FBEB of electrons from H2 or formate. Roles for HdrABC:hydrogenase complexes are also proposed for pathways wherein the methyl group of methanol is reduced to methane with electrons from H2. The HdrABC complexes catalyze FBEB-dependent oxidation of H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB. The Fdx2- supplies electrons for reduction of the methyl group to methane. In H2- independent pathways, three-fourths of the methyl groups are oxidized producing Fdx2- and reduced coenzyme F420 (F420H2). The F420H2 donates electrons for reduction of the remaining methyl groups to methane requiring transfer of electrons from Fdx2- to F420. HdrA1B1C1 is proposed to catalyze FBEB-dependent oxidation of Fdx2- for the endergonic reduction of F420 driven by the exergonic reduction of CoMS-SCoB. F420 is reduced by Rnf requiring HdrA2B2C2 catalyzing FBEB-dependent oxidation of F420H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB. The Fdx2- is recycled by Rnf and HdrA2B2C2 thereby conserving energy. The HdrA2B2C2 is also proposed to play a role in Fe(III)-dependent reverse methanogenesis. A flavin-based electron confurcating (FBEC) HdrABC complex is proposed for nitrate-dependent reverse methanogenesis in which the oxidation of CoM-SH/CoB-SH and Fdx2- is coupled to reduction of F420. The F420H2 donates electrons to a membrane complex that generates a proton gradient driving ATP synthesis. Proposed role of FBEC by HdrA1B1C1 in methylotrophic pathways of methanogenesis, overview
metabolism
-
reduction of the disulfide of coenzyme M and coenzyme B (CoMS-SCoB) by heterodisulfide reductases (HdrED and HdrABC) is the final step in all methanogenic pathways. Flavin-based electron bifurcation (FBEB) by soluble HdrABC homologues play additional roles in driving essential endergonic reactions at the expense of the exergonic reduction of CoMS-SCoM. In the first step of the CO2 reduction pathway, HdrABC complexed with hydrogenase or formate dehydrogenase generates reduced ferredoxin (Fdx2-) for the endergonic reduction of CO2 coupled to the exergonic reduction of CoMS-SCoB dependent on FBEB of electrons from H2 or formate. Roles for HdrABC:hydrogenase complexes are also proposed for pathways wherein the methyl group of methanol is reduced to methane with electrons from H2. The HdrABC complexes catalyze FBEB-dependent oxidation of H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB. The Fdx2- supplies electrons for reduction of the methyl group to methane. In H2- independent pathways, three-fourths of the methyl groups are oxidized producing Fdx2- and reduced coenzyme F420 (F420H2). The F420H2 donates electrons for reduction of the remaining methyl groups to methane requiring transfer of electrons from Fdx2- to F420. HdrA1B1C1 is proposed to catalyze FBEB-dependent oxidation of Fdx2- for the endergonic reduction of F420 driven by the exergonic reduction of CoMS-SCoB. F420 is reduced by Rnf requiring HdrA2B2C2 catalyzing FBEB-dependent oxidation of F420H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB. The Fdx2- is recycled by Rnf and HdrA2B2C2 thereby conserving energy. The HdrA2B2C2 is also proposed to play a role in Fe(III)-dependent reverse methanogenesis. A flavin-based electron confurcating (FBEC) HdrABC complex is proposed for nitrate-dependent reverse methanogenesis in which the oxidation of CoM-SH/CoB-SH and Fdx2- is coupled to reduction of F420. The F420H2 donates electrons to a membrane complex that generates a proton gradient driving ATP synthesis. Proposed role of FBEC by HdrA1B1C1 in methylotrophic pathways of methanogenesis, overview
metabolism
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reduction of the disulfide of coenzyme M and coenzyme B (CoMS-SCoB) by heterodisulfide reductases (HdrED and HdrABC) is the final step in all methanogenic pathways. Flavin-based electron bifurcation (FBEB) by soluble HdrABC homologues play additional roles in driving essential endergonic reactions at the expense of the exergonic reduction of CoMS-SCoM. In the first step of the CO2 reduction pathway, HdrABC complexed with hydrogenase or formate dehydrogenase generates reduced ferredoxin (Fdx2-) for the endergonic reduction of CO2 coupled to the exergonic reduction of CoMS-SCoB dependent on FBEB of electrons from H2 or formate. Roles for HdrABC:hydrogenase complexes are also proposed for pathways wherein the methyl group of methanol is reduced to methane with electrons from H2. The HdrABC complexes catalyze FBEB-dependent oxidation of H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB. The Fdx2- supplies electrons for reduction of the methyl group to methane. In H2- independent pathways, three-fourths of the methyl groups are oxidized producing Fdx2- and reduced coenzyme F420 (F420H2). The F420H2 donates electrons for reduction of the remaining methyl groups to methane requiring transfer of electrons from Fdx2- to F420. HdrA1B1C1 is proposed to catalyze FBEB-dependent oxidation of Fdx2- for the endergonic reduction of F420 driven by the exergonic reduction of CoMS-SCoB. F420 is reduced by Rnf requiring HdrA2B2C2 catalyzing FBEB-dependent oxidation of F420H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB. The Fdx2- is recycled by Rnf and HdrA2B2C2 thereby conserving energy. The HdrA2B2C2 is also proposed to play a role in Fe(III)-dependent reverse methanogenesis. A flavin-based electron confurcating (FBEC) HdrABC complex is proposed for nitrate-dependent reverse methanogenesis in which the oxidation of CoM-SH/CoB-SH and Fdx2- is coupled to reduction of F420. The F420H2 donates electrons to a membrane complex that generates a proton gradient driving ATP synthesis
metabolism
the oxidation of formate is catalyzed by a membrane-bound formate dehydrogenase (FdhGHI), whereas the oxidation of H2 takes place via a membrane-bound hydrogenase (VhoGAC). Based on this, the electrons fed into the anaerobic respiratory chain by FdhGHI and VhoGAC are subsequently used by a membrane-bound heterodisulfide reductase (HdrDE) to reduce the heterodisulfide (CoM-S-S-CoB), which is the terminal electron acceptor of this system, overview. Three energy-conserving, membrane-bound electron transport systems are known in methanogens: (a) H2: CoMS-S-CoB oxidoreductase (EC 1.8.98.5), (b) coenzyme F420H2: CoMS-S-CoB oxidoreductase (EC 1.8.98.4), and (c) reduced ferredoxin:CoM-S-S-CoB oxidoreductase (EC 1.8.7.3)
metabolism
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reduction of the disulfide of coenzyme M and coenzyme B (CoMS-SCoB) by heterodisulfide reductases (HdrED and HdrABC) is the final step in all methanogenic pathways. Flavin-based electron bifurcation (FBEB) by soluble HdrABC homologues play additional roles in driving essential endergonic reactions at the expense of the exergonic reduction of CoMS-SCoM. In the first step of the CO2 reduction pathway, HdrABC complexed with hydrogenase (EC 1.12.1.2) or formate dehydrogenase generates reduces ferredoxin (Fdx2-) for the endergonic reduction of CO2 coupled to the exergonic reduction of CoMS-SCoB dependent on FBEB of electrons from H2 or formate, respectively. Roles for HdrABC:hydrogenase complexes are also proposed for pathways wherein the methyl group of methanol is reduced to methane with electrons from H2. The HdrABC complexes catalyze FBEB-dependent oxidation of H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB. The Fdx2- supplies electrons for reduction of the methyl group to methane. In H2- independent pathways, threefourths of the methyl groups are oxidized producing Fdx2- and reduced coenzyme F420 (F420H2). The F420H2 donates electrons for reduction of the remaining methyl groups to methane requiring transfer of electrons from Fdx2- to F420. HdrA1B1C1 is proposed to catalyze FBEB-dependent oxidation of Fdx2- for the endergonic reduction of F420 driven by the exergonic reduction of CoMS-SCoB, see for EC 1.8.98.4. In H2- independent acetotrophic pathways (EC 1.8.98.5), the methyl group of acetate is reduced to methane with electrons derived from oxidation of the carbonyl group mediated by Fdx. Electron transport involves a membrane-bound complex (Rnf) that oxidizes Fdx2- and generates a NaC gradient driving ATP synthesis. It is postulated that F420 is reduced by Rnf requiring HdrA2B2C2 catalyzing FBEB-dependent oxidation of F420H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB (EC 1.8.98.4). The Fdx2- is recycled by Rnf and HdrA2B2C2 thereby conserving energy. The HdrA2B2C2 is also proposed to play a role in Fe(III)-dependent reverse methanogenesis. A flavin-based electron confurcating (FBEC) HdrABC complex is proposed for nitrate-dependent reverse methanogenesis in which the oxidation of CoM-SH/CoB-SH and Fdx2- is coupled to reduction of F420. The F420H2 donates electrons to a membrane complex that generates a proton gradient driving ATP synthesis
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metabolism
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reduction of the disulfide of coenzyme M and coenzyme B (CoMS-SCoB) by heterodisulfide reductases (HdrED and HdrABC) is the final step in all methanogenic pathways. Flavin-based electron bifurcation (FBEB) by soluble HdrABC homologues play additional roles in driving essential endergonic reactions at the expense of the exergonic reduction of CoMS-SCoM. In the first step of the CO2 reduction pathway, HdrABC complexed with hydrogenase (EC 1.12.1.2) or formate dehydrogenase generates reduces ferredoxin (Fdx2-) for the endergonic reduction of CO2 coupled to the exergonic reduction of CoMS-SCoB dependent on FBEB of electrons from H2 or formate, respectively. Roles for HdrABC:hydrogenase complexes are also proposed for pathways wherein the methyl group of methanol is reduced to methane with electrons from H2. The HdrABC complexes catalyze FBEB-dependent oxidation of H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB. The Fdx2- supplies electrons for reduction of the methyl group to methane. In H2- independent pathways, threefourths of the methyl groups are oxidized producing Fdx2- and reduced coenzyme F420 (F420H2). The F420H2 donates electrons for reduction of the remaining methyl groups to methane requiring transfer of electrons from Fdx2- to F420. HdrA1B1C1 is proposed to catalyze FBEB-dependent oxidation of Fdx2- for the endergonic reduction of F420 driven by the exergonic reduction of CoMS-SCoB, see for EC 1.8.98.4. In H2- independent acetotrophic pathways (EC 1.8.98.5), the methyl group of acetate is reduced to methane with electrons derived from oxidation of the carbonyl group mediated by Fdx. Electron transport involves a membrane-bound complex (Rnf) that oxidizes Fdx2- and generates a NaC gradient driving ATP synthesis. It is postulated that F420 is reduced by Rnf requiring HdrA2B2C2 catalyzing FBEB-dependent oxidation of F420H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB (EC 1.8.98.4). The Fdx2- is recycled by Rnf and HdrA2B2C2 thereby conserving energy. The HdrA2B2C2 is also proposed to play a role in Fe(III)-dependent reverse methanogenesis. A flavin-based electron confurcating (FBEC) HdrABC complex is proposed for nitrate-dependent reverse methanogenesis in which the oxidation of CoM-SH/CoB-SH and Fdx2- is coupled to reduction of F420. The F420H2 donates electrons to a membrane complex that generates a proton gradient driving ATP synthesis
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metabolism
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reduction of the disulfide of coenzyme M and coenzyme B (CoMS-SCoB) by heterodisulfide reductases (HdrED and HdrABC) is the final step in all methanogenic pathways. Flavin-based electron bifurcation (FBEB) by soluble HdrABC homologues play additional roles in driving essential endergonic reactions at the expense of the exergonic reduction of CoMS-SCoM. In the first step of the CO2 reduction pathway, HdrABC complexed with hydrogenase (EC 1.12.1.2) or formate dehydrogenase generates reduces ferredoxin (Fdx2-) for the endergonic reduction of CO2 coupled to the exergonic reduction of CoMS-SCoB dependent on FBEB of electrons from H2 or formate, respectively. Roles for HdrABC:hydrogenase complexes are also proposed for pathways wherein the methyl group of methanol is reduced to methane with electrons from H2. The HdrABC complexes catalyze FBEB-dependent oxidation of H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB. The Fdx2- supplies electrons for reduction of the methyl group to methane. In H2- independent pathways, threefourths of the methyl groups are oxidized producing Fdx2- and reduced coenzyme F420 (F420H2). The F420H2 donates electrons for reduction of the remaining methyl groups to methane requiring transfer of electrons from Fdx2- to F420. HdrA1B1C1 is proposed to catalyze FBEB-dependent oxidation of Fdx2- for the endergonic reduction of F420 driven by the exergonic reduction of CoMS-SCoB, see for EC 1.8.98.4. In H2- independent acetotrophic pathways (EC 1.8.98.5), the methyl group of acetate is reduced to methane with electrons derived from oxidation of the carbonyl group mediated by Fdx. Electron transport involves a membrane-bound complex (Rnf) that oxidizes Fdx2- and generates a NaC gradient driving ATP synthesis. It is postulated that F420 is reduced by Rnf requiring HdrA2B2C2 catalyzing FBEB-dependent oxidation of F420H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB (EC 1.8.98.4). The Fdx2- is recycled by Rnf and HdrA2B2C2 thereby conserving energy. The HdrA2B2C2 is also proposed to play a role in Fe(III)-dependent reverse methanogenesis. A flavin-based electron confurcating (FBEC) HdrABC complex is proposed for nitrate-dependent reverse methanogenesis in which the oxidation of CoM-SH/CoB-SH and Fdx2- is coupled to reduction of F420. The F420H2 donates electrons to a membrane complex that generates a proton gradient driving ATP synthesis
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metabolism
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heterodisulfide reductase plays a central role in the methanogenesis cycle of Methanococcus maripaludis
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metabolism
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in methanogens without cytochromes, the initial endergonic reduction of CO2 to formylmethanofuran with H2-derived electrons is coupled to the exergonic reduction of a heterodisulfide of coenzymes B and M by flavin-based electron bifurcation (FBEB). Methanococcus maripaludis employs three functional heterodisulfide reductase complexes for FBEB using hydrogen and formate. In Methanococcus maripaludis, FBEB is performed by a heterodisulfide reductase (Hdr) enzyme complex that involves hydrogenase (Vhu), although formate dehydrogenase (Fdh) has been proposed as an alternative to Vhu
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metabolism
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reduction of the disulfide of coenzyme M and coenzyme B (CoMS-SCoB) by heterodisulfide reductases (HdrED and HdrABC) is the final step in all methanogenic pathways. Flavin-based electron bifurcation (FBEB) by soluble HdrABC homologues play additional roles in driving essential endergonic reactions at the expense of the exergonic reduction of CoMS-SCoM. In the first step of the CO2 reduction pathway, HdrABC complexed with hydrogenase (EC 1.12.1.2) or formate dehydrogenase generates reduces ferredoxin (Fdx2-) for the endergonic reduction of CO2 coupled to the exergonic reduction of CoMS-SCoB dependent on FBEB of electrons from H2 or formate, respectively. Roles for HdrABC:hydrogenase complexes are also proposed for pathways wherein the methyl group of methanol is reduced to methane with electrons from H2. The HdrABC complexes catalyze FBEB-dependent oxidation of H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB. The Fdx2- supplies electrons for reduction of the methyl group to methane. In H2- independent pathways, threefourths of the methyl groups are oxidized producing Fdx2- and reduced coenzyme F420 (F420H2). The F420H2 donates electrons for reduction of the remaining methyl groups to methane requiring transfer of electrons from Fdx2- to F420. HdrA1B1C1 is proposed to catalyze FBEB-dependent oxidation of Fdx2- for the endergonic reduction of F420 driven by the exergonic reduction of CoMS-SCoB, see for EC 1.8.98.4. In H2- independent acetotrophic pathways (EC 1.8.98.5), the methyl group of acetate is reduced to methane with electrons derived from oxidation of the carbonyl group mediated by Fdx. Electron transport involves a membrane-bound complex (Rnf) that oxidizes Fdx2- and generates a NaC gradient driving ATP synthesis. It is postulated that F420 is reduced by Rnf requiring HdrA2B2C2 catalyzing FBEB-dependent oxidation of F420H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB (EC 1.8.98.4). The Fdx2- is recycled by Rnf and HdrA2B2C2 thereby conserving energy. The HdrA2B2C2 is also proposed to play a role in Fe(III)-dependent reverse methanogenesis. A flavin-based electron confurcating (FBEC) HdrABC complex is proposed for nitrate-dependent reverse methanogenesis in which the oxidation of CoM-SH/CoB-SH and Fdx2- is coupled to reduction of F420. The F420H2 donates electrons to a membrane complex that generates a proton gradient driving ATP synthesis
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metabolism
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reduction of the disulfide of coenzyme M and coenzyme B (CoMS-SCoB) by heterodisulfide reductases (HdrED and HdrABC) is the final step in all methanogenic pathways. Flavin-based electron bifurcation (FBEB) by soluble HdrABC homologues play additional roles in driving essential endergonic reactions at the expense of the exergonic reduction of CoMS-SCoM. In the first step of the CO2 reduction pathway, HdrABC complexed with hydrogenase (EC 1.12.1.2) or formate dehydrogenase generates reduces ferredoxin (Fdx2-) for the endergonic reduction of CO2 coupled to the exergonic reduction of CoMS-SCoB dependent on FBEB of electrons from H2 or formate, respectively. Roles for HdrABC:hydrogenase complexes are also proposed for pathways wherein the methyl group of methanol is reduced to methane with electrons from H2. The HdrABC complexes catalyze FBEB-dependent oxidation of H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB. The Fdx2- supplies electrons for reduction of the methyl group to methane. In H2- independent pathways, threefourths of the methyl groups are oxidized producing Fdx2- and reduced coenzyme F420 (F420H2). The F420H2 donates electrons for reduction of the remaining methyl groups to methane requiring transfer of electrons from Fdx2- to F420. HdrA1B1C1 is proposed to catalyze FBEB-dependent oxidation of Fdx2- for the endergonic reduction of F420 driven by the exergonic reduction of CoMS-SCoB, see for EC 1.8.98.4. In H2- independent acetotrophic pathways (EC 1.8.98.5), the methyl group of acetate is reduced to methane with electrons derived from oxidation of the carbonyl group mediated by Fdx. Electron transport involves a membrane-bound complex (Rnf) that oxidizes Fdx2- and generates a NaC gradient driving ATP synthesis. It is postulated that F420 is reduced by Rnf requiring HdrA2B2C2 catalyzing FBEB-dependent oxidation of F420H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB (EC 1.8.98.4). The Fdx2- is recycled by Rnf and HdrA2B2C2 thereby conserving energy. The HdrA2B2C2 is also proposed to play a role in Fe(III)-dependent reverse methanogenesis. A flavin-based electron confurcating (FBEC) HdrABC complex is proposed for nitrate-dependent reverse methanogenesis in which the oxidation of CoM-SH/CoB-SH and Fdx2- is coupled to reduction of F420. The F420H2 donates electrons to a membrane complex that generates a proton gradient driving ATP synthesis
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metabolism
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reduction of the disulfide of coenzyme M and coenzyme B (CoMS-SCoB) by heterodisulfide reductases (HdrED and HdrABC) is the final step in all methanogenic pathways. Flavin-based electron bifurcation (FBEB) by soluble HdrABC homologues play additional roles in driving essential endergonic reactions at the expense of the exergonic reduction of CoMS-SCoM. In the first step of the CO2 reduction pathway, HdrABC complexed with hydrogenase (EC 1.12.1.2) or formate dehydrogenase generates reduces ferredoxin (Fdx2-) for the endergonic reduction of CO2 coupled to the exergonic reduction of CoMS-SCoB dependent on FBEB of electrons from H2 or formate, respectively. Roles for HdrABC:hydrogenase complexes are also proposed for pathways wherein the methyl group of methanol is reduced to methane with electrons from H2. The HdrABC complexes catalyze FBEB-dependent oxidation of H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB. The Fdx2- supplies electrons for reduction of the methyl group to methane. In H2- independent pathways, threefourths of the methyl groups are oxidized producing Fdx2- and reduced coenzyme F420 (F420H2). The F420H2 donates electrons for reduction of the remaining methyl groups to methane requiring transfer of electrons from Fdx2- to F420. HdrA1B1C1 is proposed to catalyze FBEB-dependent oxidation of Fdx2- for the endergonic reduction of F420 driven by the exergonic reduction of CoMS-SCoB, see for EC 1.8.98.4. In H2- independent acetotrophic pathways (EC 1.8.98.5), the methyl group of acetate is reduced to methane with electrons derived from oxidation of the carbonyl group mediated by Fdx. Electron transport involves a membrane-bound complex (Rnf) that oxidizes Fdx2- and generates a NaC gradient driving ATP synthesis. It is postulated that F420 is reduced by Rnf requiring HdrA2B2C2 catalyzing FBEB-dependent oxidation of F420H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB (EC 1.8.98.4). The Fdx2- is recycled by Rnf and HdrA2B2C2 thereby conserving energy. The HdrA2B2C2 is also proposed to play a role in Fe(III)-dependent reverse methanogenesis. A flavin-based electron confurcating (FBEC) HdrABC complex is proposed for nitrate-dependent reverse methanogenesis in which the oxidation of CoM-SH/CoB-SH and Fdx2- is coupled to reduction of F420. The F420H2 donates electrons to a membrane complex that generates a proton gradient driving ATP synthesis
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metabolism
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reduction of the disulfide of coenzyme M and coenzyme B (CoMS-SCoB) by heterodisulfide reductases (HdrED and HdrABC) is the final step in all methanogenic pathways. Flavin-based electron bifurcation (FBEB) by soluble HdrABC homologues play additional roles in driving essential endergonic reactions at the expense of the exergonic reduction of CoMS-SCoM. In the first step of the CO2 reduction pathway, HdrABC complexed with hydrogenase (EC 1.12.1.2) or formate dehydrogenase generates reduces ferredoxin (Fdx2-) for the endergonic reduction of CO2 coupled to the exergonic reduction of CoMS-SCoB dependent on FBEB of electrons from H2 or formate, respectively. Roles for HdrABC:hydrogenase complexes are also proposed for pathways wherein the methyl group of methanol is reduced to methane with electrons from H2. The HdrABC complexes catalyze FBEB-dependent oxidation of H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB. The Fdx2- supplies electrons for reduction of the methyl group to methane. In H2- independent pathways, threefourths of the methyl groups are oxidized producing Fdx2- and reduced coenzyme F420 (F420H2). The F420H2 donates electrons for reduction of the remaining methyl groups to methane requiring transfer of electrons from Fdx2- to F420. HdrA1B1C1 is proposed to catalyze FBEB-dependent oxidation of Fdx2- for the endergonic reduction of F420 driven by the exergonic reduction of CoMS-SCoB, see for EC 1.8.98.4. In H2- independent acetotrophic pathways (EC 1.8.98.5), the methyl group of acetate is reduced to methane with electrons derived from oxidation of the carbonyl group mediated by Fdx. Electron transport involves a membrane-bound complex (Rnf) that oxidizes Fdx2- and generates a NaC gradient driving ATP synthesis. It is postulated that F420 is reduced by Rnf requiring HdrA2B2C2 catalyzing FBEB-dependent oxidation of F420H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB (EC 1.8.98.4). The Fdx2- is recycled by Rnf and HdrA2B2C2 thereby conserving energy. The HdrA2B2C2 is also proposed to play a role in Fe(III)-dependent reverse methanogenesis. A flavin-based electron confurcating (FBEC) HdrABC complex is proposed for nitrate-dependent reverse methanogenesis in which the oxidation of CoM-SH/CoB-SH and Fdx2- is coupled to reduction of F420. The F420H2 donates electrons to a membrane complex that generates a proton gradient driving ATP synthesis
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metabolism
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the oxidation of formate is catalyzed by a membrane-bound formate dehydrogenase (FdhGHI), whereas the oxidation of H2 takes place via a membrane-bound hydrogenase (VhoGAC). Based on this, the electrons fed into the anaerobic respiratory chain by FdhGHI and VhoGAC are subsequently used by a membrane-bound heterodisulfide reductase (HdrDE) to reduce the heterodisulfide (CoM-S-S-CoB), which is the terminal electron acceptor of this system, overview. Three energy-conserving, membrane-bound electron transport systems are known in methanogens: (a) H2: CoMS-S-CoB oxidoreductase (EC 1.8.98.5), (b) coenzyme F420H2: CoMS-S-CoB oxidoreductase (EC 1.8.98.4), and (c) reduced ferredoxin:CoM-S-S-CoB oxidoreductase (EC 1.8.7.3)
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physiological function
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HdrA1B1C1 is proposed to catalyze FBEB-dependent oxidation of Fdx2- for the endergonic reduction of F420 driven by the exergonic reduction of CoMS-SCoB. The HdrABC complexes catalyze FBEB-dependent oxidation of H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB. The Fdx2- supplies electrons for reduction of the methyl group to methane. In H2- independent pathways, three-fourths of the methyl groups are oxidized producing Fdx2- and reduced coenzyme F420 (F420H2). The F420H2 donates electrons for reduction of the remaining methyl groups to methane requiring transfer of electrons from Fdx2- to F420. HdrA1B1C1 is proposed to catalyze FBEB-dependent oxidation of Fdx2- for the endergonic reduction of F420 driven by the exergonic reduction of CoMS-SCoB
physiological function
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HdrA1B1C1 is proposed to catalyze FBEB-dependent oxidation of Fdx2- for the endergonic reduction of F420 driven by the exergonic reduction of CoMS-SCoB. The HdrABC complexes catalyze FBEB-dependent oxidation of H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB. The Fdx2- supplies electrons for reduction of the methyl group to methane. In H2- independent pathways, three-fourths of the methyl groups are oxidized producing Fdx2- and reduced coenzyme F420 (F420H2). The F420H2 donates electrons for reduction of the remaining methyl groups to methane requiring transfer of electrons from Fdx2- to F420. HdrA1B1C1 is proposed to catalyze FBEB-dependent oxidation of Fdx2- for the endergonic reduction of F420 driven by the exergonic reduction of CoMS-SCoB
physiological function
HdrA1B1C1 is proposed to catalyze FBEB-dependent oxidation of Fdx2- for the endergonic reduction of F420 driven by the exergonic reduction of CoMS-SCoB. The HdrABC complexes catalyze FBEB-dependent oxidation of H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB. The Fdx2- supplies electrons for reduction of the methyl group to methane. In H2- independent pathways, three-fourths of the methyl groups are oxidized producing Fdx2- and reduced coenzyme F420 (F420H2). The F420H2 donates electrons for reduction of the remaining methyl groups to methane requiring transfer of electrons from Fdx2- to F420. HdrA1B1C1 is proposed to catalyze FBEB-dependent oxidation of Fdx2- for the endergonic reduction of F420 driven by the exergonic reduction of CoMS-SCoB
physiological function
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HdrA1B1C1 is proposed to catalyze FBEB-dependent oxidation of Fdx2- for the endergonic reduction of F420 driven by the exergonic reduction of CoMS-SCoB. The HdrABC complexes catalyze FBEB-dependent oxidation of H2 for the endergonic reduction of Fdx driven by the exergonic reduction of CoMS-SCoB. The Fdx2- supplies electrons for reduction of the methyl group to methane. In H2- independent pathways, three-fourths of the methyl groups are oxidized producing Fdx2- and reduced coenzyme F420 (F420H2). The F420H2 donates electrons for reduction of the remaining methyl groups to methane requiring transfer of electrons from Fdx2- to F420. HdrA1B1C1 is proposed to catalyze FBEB-dependent oxidation of Fdx2- for the endergonic reduction of F420 driven by the exergonic reduction of CoMS-SCoB
physiological function
reduction of the disulfide of coenzyme M and coenzyme B (CoMS-SCoB) by heterodisulfide reductases (HdrED and HdrABC) is the final step in all methanogenic pathways. Flavin-based electron bifurcation (FBEB) by soluble HdrABC homologues play additional roles in driving essential endergonic reactions at the expense of the exergonic reduction of CoMS-SCoM
physiological function
reduction of the disulfide of coenzyme M and coenzyme B (CoMS-SCoB) by heterodisulfide reductases (HdrED and HdrABC) is the final step in all methanogenic pathways. Flavin-based electron bifurcation (FBEB) by soluble HdrABC homologues play additional roles in driving essential endergonic reactions at the expense of the exergonic reduction of CoMS-SCoM
physiological function
the energy conservation of Methanonatronarchaeum thermophilum is dependent on a respiratory chain consisting of a hydrogenase (VhoGAC, EC 1.8.98.5), a formate dehydrogenase (FdhGHI, EC 1.8.98.6), and a heterodisulfide reductase (HdrDE) that are well adapted to the harsh physicochemical conditions in the natural habitat. Methanogen Methanonatronarchaeum thermophilum is an extremely haloalkaliphilic and moderately thermophilic archaeon. A methanophenazine-like cofactor might function as an electron carrier between the hydrogenase/formate dehydrogenase and the heterodisulfide reductase. A methanophenazine-like cofactor functions as an electron carrier between the hydrogenase/formate dehydrogenase and the heterodisulfide reductase, cf. EC 1.8.98.1. The electrons fed into the anaerobic respiratory chain by FdhGHI and VhoGAC are subsequently used by a membrane-bound heterodisulfide reductase (HdrDE) to reduce the heterodisulfide (CoM-S-S-CoB), which is the terminal electron acceptor of this system
physiological function
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the HdrABC-MvhAGD enzyme complex is involved in methanogenesis from H2/CO2 using H2 as electron donor, ferredoxin (Fd) as low potential acceptor and CoM-S-S-CoB as high potential acceptor, it is involved in flavin-based electron bifurcation (FBEB). Structure-function analysis, overview
physiological function
the HdrABC-MvhAGD enzyme complex is involved in methanogenesis from H2/CO2 using H2 as electron donor, ferredoxin (Fd) as low potential acceptor and CoM-S-S-CoB as high potential acceptor, it is involved in flavin-based electron bifurcation (FBEB). Structure-function analysis, overview
physiological function
the HdrABC-MvhAGD enzyme complex is involved in methanogenesis from H2/CO2 using H2 as electron donor, ferredoxin (Fd) as low potential acceptor and CoM-S-S-CoB as high potential acceptor, it is involved in flavin-based electron bifurcation (FBEB). Structure-function analysis, overview
physiological function
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the transcriptome of Methanosarcina barkeri grown via DIET in co-culture with Geobacter metallireducens compared with its transcriptome when grown via H2 interspecies transfer (HIT) with Pelobacter carbinolicus shows that transcripts for the F420H2 dehydrogenase (Fpo) and the heterodisulfide reductase, HdrABC, are more abundant during growth on DIET. In HIT, H2 simultaneously transports both electrons and protons as the H2 diffuses between the two partners. When the H2 is oxidized in the cytoplasm with electron transfer to an electron acceptor, protons are also released and are immediately available to balance the negative charge transferred to the electron acceptor. This maintains charge balance within the cell
physiological function
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reduction of the disulfide of coenzyme M and coenzyme B (CoMS-SCoB) by heterodisulfide reductases (HdrED and HdrABC) is the final step in all methanogenic pathways. Flavin-based electron bifurcation (FBEB) by soluble HdrABC homologues play additional roles in driving essential endergonic reactions at the expense of the exergonic reduction of CoMS-SCoM
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physiological function
-
the HdrABC-MvhAGD enzyme complex is involved in methanogenesis from H2/CO2 using H2 as electron donor, ferredoxin (Fd) as low potential acceptor and CoM-S-S-CoB as high potential acceptor, it is involved in flavin-based electron bifurcation (FBEB). Structure-function analysis, overview
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physiological function
-
reduction of the disulfide of coenzyme M and coenzyme B (CoMS-SCoB) by heterodisulfide reductases (HdrED and HdrABC) is the final step in all methanogenic pathways. Flavin-based electron bifurcation (FBEB) by soluble HdrABC homologues play additional roles in driving essential endergonic reactions at the expense of the exergonic reduction of CoMS-SCoM
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physiological function
-
the HdrABC-MvhAGD enzyme complex is involved in methanogenesis from H2/CO2 using H2 as electron donor, ferredoxin (Fd) as low potential acceptor and CoM-S-S-CoB as high potential acceptor, it is involved in flavin-based electron bifurcation (FBEB). Structure-function analysis, overview
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physiological function
-
reduction of the disulfide of coenzyme M and coenzyme B (CoMS-SCoB) by heterodisulfide reductases (HdrED and HdrABC) is the final step in all methanogenic pathways. Flavin-based electron bifurcation (FBEB) by soluble HdrABC homologues play additional roles in driving essential endergonic reactions at the expense of the exergonic reduction of CoMS-SCoM
-
physiological function
-
the HdrABC-MvhAGD enzyme complex is involved in methanogenesis from H2/CO2 using H2 as electron donor, ferredoxin (Fd) as low potential acceptor and CoM-S-S-CoB as high potential acceptor, it is involved in flavin-based electron bifurcation (FBEB). Structure-function analysis, overview
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physiological function
-
reduction of the disulfide of coenzyme M and coenzyme B (CoMS-SCoB) by heterodisulfide reductases (HdrED and HdrABC) is the final step in all methanogenic pathways. Flavin-based electron bifurcation (FBEB) by soluble HdrABC homologues play additional roles in driving essential endergonic reactions at the expense of the exergonic reduction of CoMS-SCoM
-
physiological function
-
the transcriptome of Methanosarcina barkeri grown via DIET in co-culture with Geobacter metallireducens compared with its transcriptome when grown via H2 interspecies transfer (HIT) with Pelobacter carbinolicus shows that transcripts for the F420H2 dehydrogenase (Fpo) and the heterodisulfide reductase, HdrABC, are more abundant during growth on DIET. In HIT, H2 simultaneously transports both electrons and protons as the H2 diffuses between the two partners. When the H2 is oxidized in the cytoplasm with electron transfer to an electron acceptor, protons are also released and are immediately available to balance the negative charge transferred to the electron acceptor. This maintains charge balance within the cell
-
physiological function
-
the transcriptome of Methanosarcina barkeri grown via DIET in co-culture with Geobacter metallireducens compared with its transcriptome when grown via H2 interspecies transfer (HIT) with Pelobacter carbinolicus shows that transcripts for the F420H2 dehydrogenase (Fpo) and the heterodisulfide reductase, HdrABC, are more abundant during growth on DIET. In HIT, H2 simultaneously transports both electrons and protons as the H2 diffuses between the two partners. When the H2 is oxidized in the cytoplasm with electron transfer to an electron acceptor, protons are also released and are immediately available to balance the negative charge transferred to the electron acceptor. This maintains charge balance within the cell
-
physiological function
-
reduction of the disulfide of coenzyme M and coenzyme B (CoMS-SCoB) by heterodisulfide reductases (HdrED and HdrABC) is the final step in all methanogenic pathways. Flavin-based electron bifurcation (FBEB) by soluble HdrABC homologues play additional roles in driving essential endergonic reactions at the expense of the exergonic reduction of CoMS-SCoM
-
physiological function
-
the HdrABC-MvhAGD enzyme complex is involved in methanogenesis from H2/CO2 using H2 as electron donor, ferredoxin (Fd) as low potential acceptor and CoM-S-S-CoB as high potential acceptor, it is involved in flavin-based electron bifurcation (FBEB). Structure-function analysis, overview
-
physiological function
-
reduction of the disulfide of coenzyme M and coenzyme B (CoMS-SCoB) by heterodisulfide reductases (HdrED and HdrABC) is the final step in all methanogenic pathways. Flavin-based electron bifurcation (FBEB) by soluble HdrABC homologues play additional roles in driving essential endergonic reactions at the expense of the exergonic reduction of CoMS-SCoM
-
physiological function
-
the HdrABC-MvhAGD enzyme complex is involved in methanogenesis from H2/CO2 using H2 as electron donor, ferredoxin (Fd) as low potential acceptor and CoM-S-S-CoB as high potential acceptor, it is involved in flavin-based electron bifurcation (FBEB). Structure-function analysis, overview
-
physiological function
-
reduction of the disulfide of coenzyme M and coenzyme B (CoMS-SCoB) by heterodisulfide reductases (HdrED and HdrABC) is the final step in all methanogenic pathways. Flavin-based electron bifurcation (FBEB) by soluble HdrABC homologues play additional roles in driving essential endergonic reactions at the expense of the exergonic reduction of CoMS-SCoM
-
physiological function
-
the HdrABC-MvhAGD enzyme complex is involved in methanogenesis from H2/CO2 using H2 as electron donor, ferredoxin (Fd) as low potential acceptor and CoM-S-S-CoB as high potential acceptor, it is involved in flavin-based electron bifurcation (FBEB). Structure-function analysis, overview
-
physiological function
-
the energy conservation of Methanonatronarchaeum thermophilum is dependent on a respiratory chain consisting of a hydrogenase (VhoGAC, EC 1.8.98.5), a formate dehydrogenase (FdhGHI, EC 1.8.98.6), and a heterodisulfide reductase (HdrDE) that are well adapted to the harsh physicochemical conditions in the natural habitat. Methanogen Methanonatronarchaeum thermophilum is an extremely haloalkaliphilic and moderately thermophilic archaeon. A methanophenazine-like cofactor might function as an electron carrier between the hydrogenase/formate dehydrogenase and the heterodisulfide reductase. A methanophenazine-like cofactor functions as an electron carrier between the hydrogenase/formate dehydrogenase and the heterodisulfide reductase, cf. EC 1.8.98.1. The electrons fed into the anaerobic respiratory chain by FdhGHI and VhoGAC are subsequently used by a membrane-bound heterodisulfide reductase (HdrDE) to reduce the heterodisulfide (CoM-S-S-CoB), which is the terminal electron acceptor of this system
-
physiological function
Methanosarcina barkeri MS DSM 800
-
the transcriptome of Methanosarcina barkeri grown via DIET in co-culture with Geobacter metallireducens compared with its transcriptome when grown via H2 interspecies transfer (HIT) with Pelobacter carbinolicus shows that transcripts for the F420H2 dehydrogenase (Fpo) and the heterodisulfide reductase, HdrABC, are more abundant during growth on DIET. In HIT, H2 simultaneously transports both electrons and protons as the H2 diffuses between the two partners. When the H2 is oxidized in the cytoplasm with electron transfer to an electron acceptor, protons are also released and are immediately available to balance the negative charge transferred to the electron acceptor. This maintains charge balance within the cell
-
additional information
-
the enzyme complex HdrABC-MvhAGD is involved in Methanogenesis from H2/CO2. The electron-bifurcating HdrA subunit of HDRs is linked to three electron-input/-output modules: (i) the medium-potential electron donor module that may be connected via the MvhD adaptor, (ii) the high-potential, heterodisulfide-reducing HdrB electron acceptor module linked via the HdrC adaptor, and (iii) a low-potential electron acceptor module transferring electrons to ferredoxin (Fd). HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs. Disulfide intermediates other than the CoM-S-S-CoB heterodisulfide, e.g. formed by proteinogenic cysteine residues, may also be involved in catalysis of HdrA(BC) enzymes from non-methanogens. They may transfer electrons further to an additional oxidoreductase module. Architecture and function of HdrA(BC)-containing enzyme complexes, overview
additional information
the enzyme complex HdrABC-MvhAGD is involved in Methanogenesis from H2/CO2. The electron-bifurcating HdrA subunit of HDRs is linked to three electron-input/-output modules: (i) the medium-potential electron donor module that may be connected via the MvhD adaptor, (ii) the high-potential, heterodisulfide-reducing HdrB electron acceptor module linked via the HdrC adaptor, and (iii) a low-potential electron acceptor module transferring electrons to ferredoxin (Fd). HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs. Disulfide intermediates other than the CoM-S-S-CoB heterodisulfide, e.g. formed by proteinogenic cysteine residues, may also be involved in catalysis of HdrA(BC) enzymes from non-methanogens. They may transfer electrons further to an additional oxidoreductase module. Architecture and function of HdrA(BC)-containing enzyme complexes, overview
additional information
the enzyme complex HdrABC-MvhAGD is involved in Methanogenesis from H2/CO2. The electron-bifurcating HdrA subunit of HDRs is linked to three electron-input/-output modules: (i) the medium-potential electron donor module that may be connected via the MvhD adaptor, (ii) the high-potential, heterodisulfide-reducing HdrB electron acceptor module linked via the HdrC adaptor, and (iii) a low-potential electron acceptor module transferring electrons to ferredoxin (Fd). HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs. Disulfide intermediates other than the CoM-S-S-CoB heterodisulfide, e.g. formed by proteinogenic cysteine residues, may also be involved in catalysis of HdrA(BC) enzymes from non-methanogens. They may transfer electrons further to an additional oxidoreductase module. Architecture and function of HdrA(BC)-containing enzyme complexes, overview
additional information
-
when grown on formate as its sole electron donor, Methanococcus maripaludis assembles three Hdr complexes employing two Vhu domains [(Vhu)2Hdr complex], two Fdh domains [(Fdh)2Hdr complex], or one Vhu and one Fdh domain forming a heterocomplex (Fdh/Vhu/Hdr complex). Protein-protein interaction/docking analysis and modeling, usage of the crystal structure of the analogous MvhHdr complex from Methanothermococcus thermolithotrophicus (PDB ID 5ODC) as template, enzyme complex structures comparisons, overview
additional information
-
the enzyme complex HdrABC-MvhAGD is involved in Methanogenesis from H2/CO2. The electron-bifurcating HdrA subunit of HDRs is linked to three electron-input/-output modules: (i) the medium-potential electron donor module that may be connected via the MvhD adaptor, (ii) the high-potential, heterodisulfide-reducing HdrB electron acceptor module linked via the HdrC adaptor, and (iii) a low-potential electron acceptor module transferring electrons to ferredoxin (Fd). HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs. Disulfide intermediates other than the CoM-S-S-CoB heterodisulfide, e.g. formed by proteinogenic cysteine residues, may also be involved in catalysis of HdrA(BC) enzymes from non-methanogens. They may transfer electrons further to an additional oxidoreductase module. Architecture and function of HdrA(BC)-containing enzyme complexes, overview
-
additional information
-
the enzyme complex HdrABC-MvhAGD is involved in Methanogenesis from H2/CO2. The electron-bifurcating HdrA subunit of HDRs is linked to three electron-input/-output modules: (i) the medium-potential electron donor module that may be connected via the MvhD adaptor, (ii) the high-potential, heterodisulfide-reducing HdrB electron acceptor module linked via the HdrC adaptor, and (iii) a low-potential electron acceptor module transferring electrons to ferredoxin (Fd). HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs. Disulfide intermediates other than the CoM-S-S-CoB heterodisulfide, e.g. formed by proteinogenic cysteine residues, may also be involved in catalysis of HdrA(BC) enzymes from non-methanogens. They may transfer electrons further to an additional oxidoreductase module. Architecture and function of HdrA(BC)-containing enzyme complexes, overview
-
additional information
-
the enzyme complex HdrABC-MvhAGD is involved in Methanogenesis from H2/CO2. The electron-bifurcating HdrA subunit of HDRs is linked to three electron-input/-output modules: (i) the medium-potential electron donor module that may be connected via the MvhD adaptor, (ii) the high-potential, heterodisulfide-reducing HdrB electron acceptor module linked via the HdrC adaptor, and (iii) a low-potential electron acceptor module transferring electrons to ferredoxin (Fd). HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs. Disulfide intermediates other than the CoM-S-S-CoB heterodisulfide, e.g. formed by proteinogenic cysteine residues, may also be involved in catalysis of HdrA(BC) enzymes from non-methanogens. They may transfer electrons further to an additional oxidoreductase module. Architecture and function of HdrA(BC)-containing enzyme complexes, overview
-
additional information
-
when grown on formate as its sole electron donor, Methanococcus maripaludis assembles three Hdr complexes employing two Vhu domains [(Vhu)2Hdr complex], two Fdh domains [(Fdh)2Hdr complex], or one Vhu and one Fdh domain forming a heterocomplex (Fdh/Vhu/Hdr complex). Protein-protein interaction/docking analysis and modeling, usage of the crystal structure of the analogous MvhHdr complex from Methanothermococcus thermolithotrophicus (PDB ID 5ODC) as template, enzyme complex structures comparisons, overview
-
additional information
-
the enzyme complex HdrABC-MvhAGD is involved in Methanogenesis from H2/CO2. The electron-bifurcating HdrA subunit of HDRs is linked to three electron-input/-output modules: (i) the medium-potential electron donor module that may be connected via the MvhD adaptor, (ii) the high-potential, heterodisulfide-reducing HdrB electron acceptor module linked via the HdrC adaptor, and (iii) a low-potential electron acceptor module transferring electrons to ferredoxin (Fd). HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs. Disulfide intermediates other than the CoM-S-S-CoB heterodisulfide, e.g. formed by proteinogenic cysteine residues, may also be involved in catalysis of HdrA(BC) enzymes from non-methanogens. They may transfer electrons further to an additional oxidoreductase module. Architecture and function of HdrA(BC)-containing enzyme complexes, overview
-
additional information
-
the enzyme complex HdrABC-MvhAGD is involved in Methanogenesis from H2/CO2. The electron-bifurcating HdrA subunit of HDRs is linked to three electron-input/-output modules: (i) the medium-potential electron donor module that may be connected via the MvhD adaptor, (ii) the high-potential, heterodisulfide-reducing HdrB electron acceptor module linked via the HdrC adaptor, and (iii) a low-potential electron acceptor module transferring electrons to ferredoxin (Fd). HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs. Disulfide intermediates other than the CoM-S-S-CoB heterodisulfide, e.g. formed by proteinogenic cysteine residues, may also be involved in catalysis of HdrA(BC) enzymes from non-methanogens. They may transfer electrons further to an additional oxidoreductase module. Architecture and function of HdrA(BC)-containing enzyme complexes, overview
-
additional information
-
the enzyme complex HdrABC-MvhAGD is involved in Methanogenesis from H2/CO2. The electron-bifurcating HdrA subunit of HDRs is linked to three electron-input/-output modules: (i) the medium-potential electron donor module that may be connected via the MvhD adaptor, (ii) the high-potential, heterodisulfide-reducing HdrB electron acceptor module linked via the HdrC adaptor, and (iii) a low-potential electron acceptor module transferring electrons to ferredoxin (Fd). HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs. Disulfide intermediates other than the CoM-S-S-CoB heterodisulfide, e.g. formed by proteinogenic cysteine residues, may also be involved in catalysis of HdrA(BC) enzymes from non-methanogens. They may transfer electrons further to an additional oxidoreductase module. Architecture and function of HdrA(BC)-containing enzyme complexes, overview
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). HDRA_METMP
Methanococcus maripaludis (strain S2 / LL)
658
0
71281
Swiss-Prot
-
HDRA_METTH
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
659
0
72392
Swiss-Prot
-
HDRA_METTM
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)
659
0
72182
Swiss-Prot
-
HDRB1_METMP
Methanococcus maripaludis (strain S2 / LL)
301
0
33510
Swiss-Prot
-
HDRB2_METMP
Methanococcus maripaludis (strain S2 / LL)
293
0
32026
Swiss-Prot
-
HDRB_METTH
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
302
0
33513
Swiss-Prot
-
HDRB_METTM
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)
302
0
33458
Swiss-Prot
-
HDRC1_METMP
Methanococcus maripaludis (strain S2 / LL)
192
0
21600
Swiss-Prot
-
HDRC2_METMP
Methanococcus maripaludis (strain S2 / LL)
184
0
20452
Swiss-Prot
-
HDRC_METTH
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
185
0
20490
Swiss-Prot
-
HDRC_METTM
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)
185
0
20520
Swiss-Prot
-
A0A8B6SDK1_9EURY
441
0
49666
TrEMBL
-
A0A485LVC7_9ZZZZ
310
0
33418
TrEMBL
other Location (Reliability: 2)
A0A7G9Z522_9EURY
296
0
32964
TrEMBL
-
A0A8B3S270_9EURY
141
0
15989
TrEMBL
-
A0A7G9YR63_9EURY
186
0
21010
TrEMBL
-
A0A485LWP9_9ZZZZ
200
0
22565
TrEMBL
other Location (Reliability: 2)
A0A8B3S144_9EURY
198
0
22644
TrEMBL
-
A0A7G9Z592_9EURY
185
0
20995
TrEMBL
-
A0A485LW64_9ZZZZ
520
0
56536
TrEMBL
other Location (Reliability: 2)
A0A7G9Z523_9EURY
177
0
20055
TrEMBL
-
A0A8B3S0M9_9EURY
755
0
82703
TrEMBL
-
A0A485LV16_9ZZZZ
76
0
7955
TrEMBL
other Location (Reliability: 1)
A0A7G9YSM3_9EURY
232
0
26597
TrEMBL
-
A0A7G9Z591_9EURY
298
0
32950
TrEMBL
-
A0A7G9Z3C5_9EURY
62
0
6633
TrEMBL
-
A0A1Y3GAE7_9EURY
276
0
31542
TrEMBL
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterododecamer
(MvhAGD-HdrABC)2 , 1 * 72000, HdrA, + 1 * 33000, HdrB, + 1 * 21000, HdrC, + 1 * 53000, MvhA, + 1 * 34000, MvhG, + 1 * 16000, MvhD, SDS-PAGE
heterohexamer
additional information
heterohexamer
Methanobacterium thermoautotrophicus
-
2 * 80000 + 2 * 51000 + 2 * 41000 + 2 * 36000 + 2 * 21000 + 2 * 17000, SDS-PAGE
heterohexamer
Methanobacterium thermoautotrophicus DSM 2133
-
2 * 80000 + 2 * 51000 + 2 * 41000 + 2 * 36000 + 2 * 21000 + 2 * 17000, SDS-PAGE
-
additional information
-
three Hdr complexes employing two Vhu domains [(Vhu)2Hdr complex], two Fdh domains [(Fdh)2Hdr complex], or one Vhu and one Fdh domain forming a heterocomplex (Fdh/Vhu/Hdr complex)
additional information
-
three Hdr complexes employing two Vhu domains [(Vhu)2Hdr complex], two Fdh domains [(Fdh)2Hdr complex], or one Vhu and one Fdh domain forming a heterocomplex (Fdh/Vhu/Hdr complex)
-
additional information
domain structure of the HdrA dimer and MvhD, overview. Soluble HDR is composed of the three subunits HdrA, HdrB, and HdrC and is associated to a [NiFe] hydrogenase built up of three subunits termed MvhA, MvhG, and MvhD. Each HdrA consists of a central TrxR domain, the N-terminal domain, the C-terminal domain, and the Fd domain. HdrA is the catalytic subunit. Standard HdrC-like components consist of a Fd-like domain. It can be regarded as a linker module that electronically wires HdrA to HdrB by its two [4Fe-4S] clusters. HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs. The MvhD component was originally referred to as subunit of the hydrogenase component (Mvh, methyl viologen-dependent hydrogenase) in the archetypical MvhAGD-HdrABC complex
additional information
-
domain structure of the HdrA dimer and MvhD, overview. Soluble HDR is composed of the three subunits HdrA, HdrB, and HdrC and is associated to a [NiFe] hydrogenase built up of three subunits termed MvhA, MvhG, and MvhD. Each HdrA consists of a central TrxR domain, the N-terminal domain, the C-terminal domain, and the Fd domain. HdrA is the catalytic subunit. Standard HdrC-like components consist of a Fd-like domain. It can be regarded as a linker module that electronically wires HdrA to HdrB by its two [4Fe-4S] clusters. HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs. The MvhD component was originally referred to as subunit of the hydrogenase component (Mvh, methyl viologen-dependent hydrogenase) in the archetypical MvhAGD-HdrABC complex
-
additional information
-
domain structure of the HdrA dimer and MvhD, overview. Soluble HDR is composed of the three subunits HdrA, HdrB, and HdrC and is associated to a [NiFe] hydrogenase built up of three subunits termed MvhA, MvhG, and MvhD. Each HdrA consists of a central TrxR domain, the N-terminal domain, the C-terminal domain, and the Fd domain. HdrA is the catalytic subunit. Standard HdrC-like components consist of a Fd-like domain. It can be regarded as a linker module that electronically wires HdrA to HdrB by its two [4Fe-4S] clusters. HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs. The MvhD component was originally referred to as subunit of the hydrogenase component (Mvh, methyl viologen-dependent hydrogenase) in the archetypical MvhAGD-HdrABC complex
-
additional information
-
domain structure of the HdrA dimer and MvhD, overview. Soluble HDR is composed of the three subunits HdrA, HdrB, and HdrC and is associated to a [NiFe] hydrogenase built up of three subunits termed MvhA, MvhG, and MvhD. Each HdrA consists of a central TrxR domain, the N-terminal domain, the C-terminal domain, and the Fd domain. HdrA is the catalytic subunit. Standard HdrC-like components consist of a Fd-like domain. It can be regarded as a linker module that electronically wires HdrA to HdrB by its two [4Fe-4S] clusters. HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs. The MvhD component was originally referred to as subunit of the hydrogenase component (Mvh, methyl viologen-dependent hydrogenase) in the archetypical MvhAGD-HdrABC complex
-
additional information
-
domain structure of the HdrA dimer and MvhD, overview. Soluble HDR is composed of the three subunits HdrA, HdrB, and HdrC and is associated to a [NiFe] hydrogenase built up of three subunits termed MvhA, MvhG, and MvhD. Each HdrA consists of a central TrxR domain, the N-terminal domain, the C-terminal domain, and the Fd domain. HdrA is the catalytic subunit. Standard HdrC-like components consist of a Fd-like domain. It can be regarded as a linker module that electronically wires HdrA to HdrB by its two [4Fe-4S] clusters. HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs. The MvhD component was originally referred to as subunit of the hydrogenase component (Mvh, methyl viologen-dependent hydrogenase) in the archetypical MvhAGD-HdrABC complex
-
additional information
-
domain structure of the HdrA dimer and MvhD, overview. Soluble HDR is composed of the three subunits HdrA, HdrB, and HdrC and is associated to a [NiFe] hydrogenase built up of three subunits termed MvhA, MvhG, and MvhD. Each HdrA consists of a central TrxR domain, the N-terminal domain, the C-terminal domain, and the Fd domain. HdrA is the catalytic subunit. Standard HdrC-like components consist of a Fd-like domain. It can be regarded as a linker module that electronically wires HdrA to HdrB by its two [4Fe-4S] clusters. HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs. The MvhD component was originally referred to as subunit of the hydrogenase component (Mvh, methyl viologen-dependent hydrogenase) in the archetypical MvhAGD-HdrABC complex
-
additional information
-
domain structure of the HdrA dimer and MvhD, overview. Soluble HDR is composed of the three subunits HdrA, HdrB, and HdrC and is associated to a [NiFe] hydrogenase built up of three subunits termed MvhA, MvhG, and MvhD. Each HdrA consists of a central TrxR domain, the N-terminal domain, the C-terminal domain, and the Fd domain. HdrA is the catalytic subunit. Standard HdrC-like components consist of a Fd-like domain. It can be regarded as a linker module that electronically wires HdrA to HdrB by its two [4Fe-4S] clusters. HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs. The MvhD component was originally referred to as subunit of the hydrogenase component (Mvh, methyl viologen-dependent hydrogenase) in the archetypical MvhAGD-HdrABC complex
-
additional information
-
domain structure of the HdrA dimer and MvhD, overview. Soluble HDR is composed of the three subunits HdrA, HdrB, and HdrC and is associated to a [NiFe] hydrogenase built up of three subunits termed MvhA, MvhG, and MvhD. Each HdrA consists of a central TrxR domain, the N-terminal domain, the C-terminal domain, and the Fd domain. HdrA is the catalytic subunit. Standard HdrC-like components consist of a Fd-like domain. It can be regarded as a linker module that electronically wires HdrA to HdrB by its two [4Fe-4S] clusters. HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs. The MvhD component was originally referred to as subunit of the hydrogenase component (Mvh, methyl viologen-dependent hydrogenase) in the archetypical MvhAGD-HdrABC complex
additional information
domain structure of the HdrA dimer and MvhD, overview. Soluble HDR is composed of the three subunits HdrA (72 kDa), HdrB (33 kDa) and HdrC (21 kDa) and is associated to a [NiFe] hydrogenase built up of three subunits termed MvhA (53 kDa), MvhG (34 kDa) and MvhD (16 kDa). Each HdrA consists of a central TrxR domain, the N-terminal domain, the C-terminal domain, and the Fd domain. HdrA is the catalytic subunit. Standard HdrC-like components consist of a Fd-like domain. It can be regarded as a linker module that electronically wires HdrA to HdrB by its two [4Fe-4S] clusters. HdrB-like components contain a conserved cysteine-rich motif, referred to as CCG domain that is involved in binding two unique non-cubane [4Fe-4S] clusters. They are directly involved in heterodisulfide reduction in the active site of HDRs. The MvhD component was originally referred to as subunit of the hydrogenase component (Mvh, methyl viologen-dependent hydrogenase) in the archetypical MvhAGD-HdrABC complex
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis of the heterododecameric enzyme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose and Q-Sepharose column chromatography, and Superdex 200 gel filtration
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DEAE-Sepharose column chromatography, phenyl-Sepharose column chromatography, and hydroxyapatite column chromatography
Methanobacterium thermoautotrophicus
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DEAE-Sepharose column chromatography, Q-Sepharose column chromatography, and Superdex 200 gel filtration
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recombinant His-tagged enzyme complex components, Fdh, Vhu, and Hdr from Escherichia coli by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of His-tagged enzyme complex components, Fdh, Vhu, and Hdr in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kaster, A.; Moll, J.; Parey, K.; Thauer, R.
Coupling of ferredoxin and heterodisulfide reduction via electron bifurcation in hydrogenotrophic methanogenic archaea
Proc. Natl. Acad. Sci. USA
108
2981-2986
2011
Methanothermobacter marburgensis (Q50754), Methanothermobacter marburgensis (Q50755), Methanothermobacter marburgensis (Q50756), Methanothermobacter marburgensis, Methanothermobacter marburgensis DSM 2133 (Q50754), Methanothermobacter marburgensis DSM 2133 (Q50755), Methanothermobacter marburgensis DSM 2133 (Q50756)
brenda
Stojanowic, A.; Mander, G.; Duin, E.; Hedderich, R.
Physiological role of the F420-non-reducing hydrogenase (MvH) from Methanothermobacter marburgensis
Arch. Microbiol.
180
194-203
2003
Methanothermobacter marburgensis, Methanothermobacter marburgensis DSM 2133
brenda
Setzke, E.; Hedderich, R.; Heiden, S.; Thauer, R.
H2 heterodisulfide oxidoreductase complex from Methanobacterium thermoautotrophicum Composition and properties
Eur. J. Biochem.
220
139-148
1994
Methanobacterium thermoautotrophicus, Methanobacterium thermoautotrophicus DSM 2133
brenda
Kaster, A.; Moll, J.; Parey, K.; Thauer, R.
Coupling of ferredoxin and heterodisulfide reduction via electron bifurcation in hydrogenotrophic methanogenic archaea
Proc. Natl. Acad. Sci. USA
108
2981-2986
2011
Methanothermobacter marburgensis, Methanothermobacter marburgensis DSM 2133
brenda
Milton, R.; Ruth, J.; Deutzmann, J.; Spormann, A.
Methanococcus maripaludis employs three functional heterodisulfide reductase complexes for flavin-based electron bifurcation using hydrogen and formate
Biochemistry
57
4848-4857
2018
Methanococcus maripaludis, Methanococcus maripaludis LL
brenda
Appel, L.; Willistein, M.; Dahl, C.; Ermler, U.; Boll, M.
Functional diversity of prokaryotic HdrA(BC) modules Role in flavin-based electron bifurcation processes and beyond
Biochim. Biophys. Acta
1862
148379
2021
Methanothermobacter wolfeii, Methanothermococcus thermolithotrophicus (A0A2D0TCB9 AND A0A2D0TCB4 AND A0A2D0TC97 AND A0A2D0TCA6 AND A0A2D0TC99 AND A0A2D0TC98), Methanothermobacter marburgensis (Q50756 AND Q50755 AND Q50754 AND P60227 AND P60239 AND P60238), Methanothermobacter marburgensis Marburg (Q50756 AND Q50755 AND Q50754 AND P60227 AND P60239 AND P60238), Methanothermobacter marburgensis ATCC BAA-927 (Q50756 AND Q50755 AND Q50754 AND P60227 AND P60239 AND P60238), Methanothermobacter marburgensis NBRC 100331 (Q50756 AND Q50755 AND Q50754 AND P60227 AND P60239 AND P60238), Methanothermobacter marburgensis JCM 14651 (Q50756 AND Q50755 AND Q50754 AND P60227 AND P60239 AND P60238), Methanothermobacter marburgensis DSM 2133 (Q50756 AND Q50755 AND Q50754 AND P60227 AND P60239 AND P60238), Methanothermobacter marburgensis OCM 82 (Q50756 AND Q50755 AND Q50754 AND P60227 AND P60239 AND P60238)
brenda
Steiniger, F.; Sorokin, D.; Deppenmeier, U.
Process of energy conservation in the extremely haloalkaliphilic methyl-reducing methanogen Methanonatronarchaeum thermophilum
FEBS J.
289
549-563
2022
Methanonatronarchaeum thermophilum (A0A1Y3GAE7), Methanonatronarchaeum thermophilum AMET1 (A0A1Y3GAE7)
brenda
Yan, Z.; Ferry, J.
Electron bifurcation and confurcation in methanogenesis and reverse methanogenesis
Front. Microbiol.
9
1322
2018
Methanothermococcus thermolithotrophicus, Methanosarcina acetivorans, Methanothermobacter marburgensis, Methanothermobacter marburgensis (Q50756 AND Q50755 AND Q50754), Methanocella conradii, no activity in Methanomassiliicoccus luminyensis, Methanococcus maripaludis (Q6LWL2 AND Q6LY38 AND Q6LYD8 AND Q6LY39 AND Q6LYD7), Methanothermobacter marburgensis Marburg (Q50756 AND Q50755 AND Q50754), Methanothermobacter marburgensis ATCC BAA-927 (Q50756 AND Q50755 AND Q50754), Methanothermobacter marburgensis NBRC 100331 (Q50756 AND Q50755 AND Q50754), Methanococcus maripaludis LL (Q6LWL2 AND Q6LY38 AND Q6LYD8 AND Q6LY39 AND Q6LYD7), Methanothermobacter marburgensis JCM 14651 (Q50756 AND Q50755 AND Q50754), Methanothermobacter marburgensis DSM 2133 (Q50756 AND Q50755 AND Q50754), Methanothermobacter marburgensis OCM 82 (Q50756 AND Q50755 AND Q50754)
brenda
Holmes, D.; Rotaru, A.; Ueki, T.; Shrestha, P.; Ferry, J.; Lovley, D.
Electron and proton flux for carbon dioxide reduction in Methanosarcina barkeri during direct interspecies electron transfer
Front. Microbiol.
9
3109
2018
Methanosarcina barkeri, Methanosarcina barkeri MS DSM 800
brenda
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Release 2023.1 (January 2023)
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