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Literature summary for 1.8.7.3 extracted from

  • Wagner, T.; Koch, J.; Ermler, U.; Shima, S.
    Methanogenic heterodisulfide reductase (HdrABC-MvhAGD) uses two noncubane [4Fe-4S] clusters for reduction (2017), Science, 357, 699-703 .
    View publication on PubMed

Application

Application Comment Organism
additional information the HdrABC-MvhAGD atomic model serves as a structural template for numerous HdrABC homologs involved in diverse microbial metabolic pathways Methanothermobacter wolfeii
additional information the HdrABC-MvhAGD atomic model serves as a structural template for numerous HdrABC homologs involved in diverse microbial metabolic pathways Methanothermococcus thermolithotrophicus
additional information the HdrABC-MvhAGD atomic model serves as a structural template for numerous HdrABC homologs involved in diverse microbial metabolic pathways Methanocaldococcus jannaschii

Crystallization (Commentary)

Crystallization (Comment) Organism
purified HdrABC-MvhAGD complex, X-ray diffraction structure determination and analysis at 2.15 A resolution Methanothermococcus thermolithotrophicus
purified HdrABC-MvhAGD complex, X-ray diffraction structure determination and analysis at 4.35 A resolution Methanothermobacter wolfeii

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Methanothermobacter wolfeii 16020
-
membrane
-
Methanothermococcus thermolithotrophicus 16020
-
membrane
-
Methanocaldococcus jannaschii 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ in two noncubane [4Fe-4S] clusters of HdrB. The two noncubane [4Fe-4S] clusters are composed of fused [3Fe-4S]-[2Fe-2S] units sharing 1 iron and 1 sulfur, which are coordinated at the CCG motifs Methanothermobacter wolfeii
Fe2+ in two noncubane [4Fe-4S] clusters of HdrB. The two noncubane [4Fe-4S] clusters are composed of fused [3Fe-4S]-[2Fe-2S] units sharing 1 iron and 1 sulfur, which are coordinated at the CCG motifs Methanothermococcus thermolithotrophicus
Fe2+ in two noncubane [4Fe-4S] clusters of HdrB. The two noncubane [4Fe-4S] clusters are composed of fused [3Fe-4S]-[2Fe-2S] units sharing 1 iron and 1 sulfur, which are coordinated at the CCG motifs Methanocaldococcus jannaschii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + 2 H+ Methanothermobacter wolfeii
-
2 oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + 2 H+ Methanothermococcus thermolithotrophicus
-
2 oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + 2 H+ Methanocaldococcus jannaschii
-
2 oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + 2 H+ Methanocaldococcus jannaschii NBRC 100440
-
2 oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + 2 H+ Methanocaldococcus jannaschii DSM 2661
-
2 oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + 2 H+ Methanocaldococcus jannaschii ATCC 43067
-
2 oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + 2 H+ Methanocaldococcus jannaschii JAL-1
-
2 oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + 2 H+ Methanothermococcus thermolithotrophicus DSM 2095
-
2 oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + 2 H+ Methanocaldococcus jannaschii JCM 10045
-
2 oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
-
?

Organism

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii P60200 AND Q58153 AND Q58273 AND Q58154 AND Q58274 CoB-CoM heterodisulfide reductase subunits A, B1, B2, C1, and C2; Methanococcus jannaschii
-
Methanocaldococcus jannaschii ATCC 43067 P60200 AND Q58153 AND Q58273 AND Q58154 AND Q58274 CoB-CoM heterodisulfide reductase subunits A, B1, B2, C1, and C2; Methanococcus jannaschii
-
Methanocaldococcus jannaschii DSM 2661 P60200 AND Q58153 AND Q58273 AND Q58154 AND Q58274 CoB-CoM heterodisulfide reductase subunits A, B1, B2, C1, and C2; Methanococcus jannaschii
-
Methanocaldococcus jannaschii JAL-1 P60200 AND Q58153 AND Q58273 AND Q58154 AND Q58274 CoB-CoM heterodisulfide reductase subunits A, B1, B2, C1, and C2; Methanococcus jannaschii
-
Methanocaldococcus jannaschii JCM 10045 P60200 AND Q58153 AND Q58273 AND Q58154 AND Q58274 CoB-CoM heterodisulfide reductase subunits A, B1, B2, C1, and C2; Methanococcus jannaschii
-
Methanocaldococcus jannaschii NBRC 100440 P60200 AND Q58153 AND Q58273 AND Q58154 AND Q58274 CoB-CoM heterodisulfide reductase subunits A, B1, B2, C1, and C2; Methanococcus jannaschii
-
Methanothermobacter wolfeii
-
-
-
Methanothermococcus thermolithotrophicus A0A2D0TCB9 AND A0A2D0TCB4 AND A0A2D0TC97 CoB-CoM heterodisulfide reductase subunits A, B, and C
-
Methanothermococcus thermolithotrophicus DSM 2095 A0A2D0TCB9 AND A0A2D0TCB4 AND A0A2D0TC97 CoB-CoM heterodisulfide reductase subunits A, B, and C
-

Reaction

Reaction Comment Organism Reaction ID
2 oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM = 2 reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + 2 H+ subunit HdrB of heterodisulfide reductase (HdrABC-MvhAGD) contains two noncubane [4Fe-4S] clusters tht are involved in reduction activity. The heterodisulfide is clamped between the two noncubane [4Fe-4S] clusters and homolytically cleaved, forming coenzyme M and B bound to each iron. Coenzymes are consecutively released upon one-by-one electron transfer Methanothermobacter wolfeii
2 oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM = 2 reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + 2 H+ subunit HdrB of heterodisulfide reductase (HdrABC-MvhAGD) contains two noncubane [4Fe-4S] clusters tht are involved in reduction activity. The heterodisulfide is clamped between the two noncubane [4Fe-4S] clusters and homolytically cleaved, forming coenzyme M and B bound to each iron. Coenzymes are consecutively released upon one-by-one electron transfer Methanothermococcus thermolithotrophicus
2 oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM = 2 reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + 2 H+ subunit HdrB of heterodisulfide reductase (HdrABC-MvhAGD) contains two noncubane [4Fe-4S] clusters tht are involved in reduction activity. The heterodisulfide is clamped between the two noncubane [4Fe-4S] clusters and homolytically cleaved, forming coenzyme M and B bound to each iron. Coenzymes are consecutively released upon one-by-one electron transfer Methanocaldococcus jannaschii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + 2 H+
-
Methanothermobacter wolfeii 2 oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + 2 H+
-
Methanothermococcus thermolithotrophicus 2 oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + 2 H+
-
Methanocaldococcus jannaschii 2 oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + 2 H+
-
Methanocaldococcus jannaschii NBRC 100440 2 oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + 2 H+
-
Methanocaldococcus jannaschii DSM 2661 2 oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + 2 H+
-
Methanocaldococcus jannaschii ATCC 43067 2 oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + 2 H+
-
Methanocaldococcus jannaschii JAL-1 2 oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + 2 H+
-
Methanothermococcus thermolithotrophicus DSM 2095 2 oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
-
?
2 reduced ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB + 2 H+
-
Methanocaldococcus jannaschii JCM 10045 2 oxidized ferredoxin [iron-sulfur] cluster + CoB + CoM
-
?

Subunits

Subunits Comment Organism
oligomer structure analysis of the native heterododecameric HdrABC-MvhAGD complex, overview. The multisubunit enzyme complex is composed of a dimer of two HdrABC-MvhAGD heterohexamers with a flavin-containing HdrA dimer in the center, to which two catalytic arms, MvhAGD and HdrBC, are attached Methanocaldococcus jannaschii
oligomer structure analysis of the native heterododecameric HdrABC-MvhAGD complex, overview. The multisubunit enzyme complex is composed of a dimer of two HdrABC-MvhAGD heterohexamers with a flavin-containing HdrA dimer in the center, to which two catalytic arms, MvhAGD and HdrBC, are attached. HdrA is tightly associated with HdrA' (amino acid residues of the partner protomer are marked with an apostrophe) and comprises anN-terminal (1 to 133), a thioredoxin-reductase (145 to 236 and 315 to 567), an inserted ferredoxin (237 to 314), and a C-terminal ferredoxin domain (568 to 654) Methanothermococcus thermolithotrophicus
oligomer the multisubunit enzyme complex is composed of a dimer of two HdrABC-MvhAGD heterohexamers with a flavin-containing HdrA dimer in the center, to which two catalytic arms, MvhAGD and HdrBC, are attached Methanothermobacter wolfeii

Synonyms

Synonyms Comment Organism
HdrABC
-
Methanothermobacter wolfeii
HdrABC
-
Methanothermococcus thermolithotrophicus
HdrABC
-
Methanocaldococcus jannaschii
heterodisulfide reductase
-
Methanothermobacter wolfeii
heterodisulfide reductase
-
Methanothermococcus thermolithotrophicus
heterodisulfide reductase
-
Methanocaldococcus jannaschii
More cf. EC 1.8.98.1, EC 1.8.98.4, and EC 1.8.98.5 Methanothermobacter wolfeii
More cf. EC 1.8.98.1, EC 1.8.98.4, and EC 1.8.98.5 Methanothermococcus thermolithotrophicus
More cf. EC 1.8.98.1, EC 1.8.98.4, and EC 1.8.98.5 Methanocaldococcus jannaschii

Cofactor

Cofactor Comment Organism Structure
FAD the multisubunit enzyme complex is composed of a dimer of two HdrABC-MvhAGD heterohexamers with a flavin-containing HdrA dimer in the center, to which two catalytic arms, MvhAGD and HdrBC, are attached Methanothermobacter wolfeii
FAD the multisubunit enzyme complex is composed of a dimer of two HdrABC-MvhAGD heterohexamers with a flavin-containing HdrA dimer in the center, to which two catalytic arms, MvhAGD and HdrBC, are attached Methanothermococcus thermolithotrophicus
FAD the multisubunit enzyme complex is composed of a dimer of two HdrABC-MvhAGD heterohexamers with a flavin-containing HdrA dimer in the center, to which two catalytic arms, MvhAGD and HdrBC, are attached Methanocaldococcus jannaschii
Fe-S center subunits HdrB of heterodisulfide reductase (HdrABC-MvhAGD) contains two noncubane [4Fe-4S] clusters used for reduction activity. The two noncubane [4Fe-4S] clusters are composed of fused [3Fe-4S]-[2Fe-2S] units sharing 1 iron (Fe) and 1 sulfur (S), which are coordinated at the CCG motifs. The N-terminal domain has a fold similar to MvhD but contains, instead of a [2Fe-2S] cluster, a [4Fe-4S] cluster (HA3) that is unusually ligated by five cysteines Methanothermobacter wolfeii
Fe-S center subunits HdrB of heterodisulfide reductase (HdrABC-MvhAGD) contains two noncubane [4Fe-4S] clusters used for reduction activity. The two noncubane [4Fe-4S] clusters are composed of fused [3Fe-4S]-[2Fe-2S] units sharing 1 iron (Fe) and 1 sulfur (S), which are coordinated at the CCG motifs. The N-terminal domain has a fold similar to MvhD but contains, instead of a [2Fe-2S] cluster, a [4Fe-4S] cluster (HA3) that is unusually ligated by five cysteines Methanothermococcus thermolithotrophicus
Fe-S center subunits HdrB of heterodisulfide reductase (HdrABC-MvhAGD) contains two noncubane [4Fe-4S] clusters used for reduction activity. The two noncubane [4Fe-4S] clusters are composed of fused [3Fe-4S]-[2Fe-2S] units sharing 1 iron and 1 sulfur, which are coordinated at the CCG motifs. The N-terminal domain has a fold similar to MvhD but contains, instead of a [2Fe-2S] cluster, a [4Fe-4S] cluster (HA3) that is unusually ligated by five cysteines Methanocaldococcus jannaschii
additional information the thioredoxin reductase domain of HdrA (145 to 236 and 315 to 567) resembles thioredoxin reductase in the fold and geometry of the FAD-binding site but forms a completely different dimer interface, owing to the perpendicular position of the respective two-fold axes. The thioredoxin-reductase domain of HdrA has, in addition, a [4Fe-4S] cluster (HA4) that is surrounded by several basic residues and coordinated with a Cys386, Cys399, Cys403, and Cys404 sequence motif (consensus sequence CX10-16-Y/W/H/F-C-S/A/C-X2-3CC) Methanothermobacter wolfeii
additional information the thioredoxin reductase domain of HdrA (145 to 236 and 315 to 567) resembles thioredoxin reductase in the fold and geometry of the FAD-binding site but forms a completely different dimer interface, owing to the perpendicular position of the respective two-fold axes. The thioredoxin-reductase domain of HdrA has, in addition, a [4Fe-4S] cluster (HA4) that is surrounded by several basic residues and coordinated with a Cys386, Cys399, Cys403, and Cys404 sequence motif (consensus sequence CX10-16-Y/W/H/F-C-S/A/C-X2-3CC) Methanothermococcus thermolithotrophicus
additional information the thioredoxin reductase domain of HdrA (145 to 236 and 315 to 567) resembles thioredoxin reductase in the fold and geometry of the FAD-binding site but forms a completely different dimer interface, owing to the perpendicular position of the respective two-fold axes. The thioredoxin-reductase domain of HdrA has, in addition, a [4Fe-4S] cluster (HA4) that is surrounded by several basic residues and coordinated with a Cys386, Cys399, Cys403, and Cys404 sequence motif (consensus sequence CX10-16-Y/W/H/F-C-S/A/C-X2-3CC) Methanocaldococcus jannaschii

General Information

General Information Comment Organism
evolution HdrA homologues are found in many other microorganisms, i.e. anaerobic methanotrophic archaea, sulfate-reducing bacteria and archaea, sulfur-oxidizing bacteria, acetogenic bacteria, knallgas bacteria, and metal-reducing bacteria Methanothermobacter wolfeii
evolution HdrA homologues are found in many other microorganisms, i.e. anaerobic methanotrophic archaea, sulfate-reducing bacteria and archaea, sulfur-oxidizing bacteria, acetogenic bacteria, knallgas bacteria, and metal-reducing bacteria. The fifth cysteine Cys197' of Methanothermococcus thermolithotrophicus HdrA is exchanged for a selenocysteine in HdrA from Methanocaldococcus jannaschii Methanothermococcus thermolithotrophicus
evolution HdrA homologues are found in many other microorganisms, i.e. anaerobic methanotrophic archaea, sulfate-reducing bacteria and archaea, sulfur-oxidizing bacteria, acetogenic bacteria, knallgas bacteria, and metal-reducing bacteria. The fifth cysteine Cys197' of Methanothermococcus thermolithotrophicus HdrA is exchanged for a selenocysteine in HdrA from Methanocaldococcus jannaschii Methanocaldococcus jannaschii
metabolism in methanogenic archaea, the carbon dioxide (CO2) fixation and methane-forming steps are linked through the heterodisulfide reductase (HdrABC)-[NiFe]-hydrogenase (MvhAGD) complex that uses flavin-based electron bifurcation to reduce ferredoxin and the heterodisulfide of coenzymes M and B Methanothermobacter wolfeii
metabolism in methanogenic archaea, the carbon dioxide (CO2) fixation and methane-forming steps are linked through the heterodisulfide reductase (HdrABC)-[NiFe]-hydrogenase (MvhAGD) complex that uses flavin-based electron bifurcation to reduce ferredoxin and the heterodisulfide of coenzymes M and B Methanothermococcus thermolithotrophicus
metabolism in methanogenic archaea, the carbon dioxide (CO2) fixation and methane-forming steps are linked through the heterodisulfide reductase (HdrABC)-[NiFe]-hydrogenase (MvhAGD) complex that uses flavin-based electron bifurcation to reduce ferredoxin and the heterodisulfide of coenzymes M and B Methanocaldococcus jannaschii
additional information the methanogenic heterodisulfide reductase (HdrABC-MvhAGD) uses two noncubane [4Fe-4S] clusters for reduction. Analysis of the structure of the native heterododecameric HdrABC-MvhAGD complex at 2.15 A resolution. Subunit HdrB of heterodisulfide reductase (HdrABC-MvhAGD) contains two noncubane [4Fe-4S] clusters tht are involved in reduction activity. The heterodisulfide is clamped between the two noncubane [4Fe-4S] clusters and homolytically cleaved, forming coenzyme M and B bound to each iron. Coenzymes are consecutively released upon one-by-one electron transfer. The HdrABC-MvhAGD atomic model serves as a structural template for numerous HdrABC homologs involved in diverse microbial metabolic pathways. The multisubunit enzyme complex is composed of a dimer of two HdrABC-MvhAGD heterohexamers with a flavin-containing HdrA dimer in the center, to which two catalytic arms, MvhAGD and HdrBC, are attached. MvhA and MvhG are homologous to the large and small subunits of [NiFe] hydrogenase (EC 1.12.7.2), respectively. The thioredoxin reductase domain of HdrA (145 to 236 and 315 to 567) resembles thioredoxin reductase in the fold and geometry of the FAD-binding site but forms a completely different dimer interface, owing to the perpendicular position of the respective two-fold axes. The thioredoxin-reductase domain of HdrA has, in addition, a [4Fe-4S] cluster (HA4) that is surrounded by several basic residues and coordinated with a Cys386, Cys399, Cys403, and Cys404 sequence motif (consensus sequence CX10-16-Y/W/H/F-C-S/A/C-X2-3CC). HdrB is unusual in that spectroscopic studies have suggested that disulfide reduction occurs through two one-electron steps rather than the typical two-electron step. HdrB contains a duplicated CCG motif with the sequence CX31-39CCX35-36CXXC. This motif is predicted to be a binding motif for iron-sulfur clusters, which occurs in numerous microbes. Structure comparisons Methanothermobacter wolfeii
additional information the methanogenic heterodisulfide reductase (HdrABC-MvhAGD) uses two noncubane [4Fe-4S] clusters for reduction. Analysis of the structure of the native heterododecameric HdrABC-MvhAGD complex at 2.15 A resolution. Subunit HdrB of heterodisulfide reductase (HdrABC-MvhAGD) contains two noncubane [4Fe-4S] clusters tht are involved in reduction activity. The heterodisulfide is clamped between the two noncubane [4Fe-4S] clusters and homolytically cleaved, forming coenzyme M and B bound to each iron. Coenzymes are consecutively released upon one-by-one electron transfer. The HdrABC-MvhAGD atomic model serves as a structural template for numerous HdrABC homologs involved in diverse microbial metabolic pathways. The multisubunit enzyme complex is composed of a dimer of two HdrABC-MvhAGD heterohexamers with a flavin-containing HdrA dimer in the center, to which two catalytic arms, MvhAGD and HdrBC, are attached. MvhA and MvhG are homologous to the large and small subunits of [NiFe] hydrogenase (EC 1.12.7.2), respectively. The thioredoxin reductase domain of HdrA (145 to 236 and 315 to 567) resembles thioredoxin reductase in the fold and geometry of the FAD-binding site but forms a completely different dimer interface, owing to the perpendicular position of the respective two-fold axes. The thioredoxin-reductase domain of HdrA has, in addition, a [4Fe-4S] cluster (HA4) that is surrounded by several basic residues and coordinated with a Cys386, Cys399, Cys403, and Cys404 sequence motif (consensus sequence CX10-16-Y/W/H/F-C-S/A/C-X2-3CC). HdrB is unusual in that spectroscopic studies have suggested that disulfide reduction occurs through two one-electron steps rather than the typical two-electron step. HdrB contains a duplicated CCG motif with the sequence CX31-39CCX35-36CXXC. This motif is predicted to be a binding motif for iron-sulfur clusters, which occurs in numerous microbes. Structure comparisons Methanocaldococcus jannaschii
additional information the methanogenic heterodisulfide reductase (HdrABC-MvhAGD) uses two noncubane [4Fe-4S] clusters for reduction. Analysis of the structure of the native heterododecameric HdrABC-MvhAGD complex at 2.15 A resolution. Subunit HdrB of heterodisulfide reductase (HdrABC-MvhAGD) contains two noncubane [4Fe-4S] clusters tht are involved in reduction activity. The heterodisulfide is clamped between the two noncubane [4Fe-4S] clusters and homolytically cleaved, forming coenzyme M and B bound to each iron. Coenzymes are consecutively released upon one-by-one electron transfer. The HdrABC-MvhAGD atomic model serves as a structural template for numerous HdrABC homologs involved in diverse microbial metabolic pathways. The multisubunit enzyme complex is composed of a dimer of two HdrABC-MvhAGD heterohexamers with a flavin-containing HdrA dimer in the center, to which two catalytic arms, MvhAGD and HdrBC, are attached. MvhA and MvhG are homologous to the large and small subunits of [NiFe] hydrogenase (EC 1.12.7.2), respectively. The thioredoxin reductase domain of HdrA (145 to 236 and 315 to 567) resembles thioredoxin reductase in the fold and geometry of the FAD-binding site but forms a completely different dimer interface, owing to the perpendicular position of the respective two-fold axes. The thioredoxin-reductase domain of HdrA has, in addition, a [4Fe-4S] cluster (HA4) that is surrounded by several basic residues and coordinated with a Cys386, Cys399, Cys403, and Cys404 sequence motif (consensus sequence CX10-16-Y/W/H/F-C-S/A/C-X2-3CC). HdrB is unusual in that spectroscopic studies have suggested that disulfide reduction occurs through two one-electron steps rather than the typical two-electron step. HdrB contains a duplicated CCG motif with the sequence CX31-39CCX35-36CXXC. This motif is predicted to be a binding motif for iron-sulfur clusters, which occurs in numerous microbes. Structure comparisons. Structure-function anaysis, detailed overview Methanothermococcus thermolithotrophicus
physiological function the HdrABC-MvhAGD complex catalyzes an iron-sulfur cluster-assisted disulfide reduction reaction. This reaction is integrated into a flavin-based electron bifurcation (FBEB) process, a mode of energy coupling that optimizes the energy yield of the cell. The key subunits are HdrA, which carries the electron-bifurcating flavin adenine dinucleotide (FAD), and HdrB, which has been proposed to be the heterodisulfide reductase site Methanothermobacter wolfeii
physiological function the HdrABC-MvhAGD complex catalyzes an iron-sulfur cluster-assisted disulfide reduction reaction. This reaction is integrated into a flavin-based electron bifurcation (FBEB) process, a mode of energy coupling that optimizes the energy yield of the cell. The key subunits are HdrA, which carries the electron-bifurcating flavin adenine dinucleotide (FAD), and HdrB, which has been proposed to be the heterodisulfide reductase site Methanothermococcus thermolithotrophicus
physiological function the HdrABC-MvhAGD complex catalyzes an iron-sulfur cluster-assisted disulfide reduction reaction. This reaction is integrated into a flavin-based electron bifurcation (FBEB) process, a mode of energy coupling that optimizes the energy yield of the cell. The key subunits are HdrA, which carries the electron-bifurcating flavin adenine dinucleotide (FAD), and HdrB, which has been proposed to be the heterodisulfide reductase site Methanocaldococcus jannaschii