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Literature summary for 1.8.98.6 extracted from

  • 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 (2018), Biochemistry, 57, 4848-4857 .
    View publication on PubMed
Search for more literature for 1.8.98.6

Activating Compound

Activating Compound Comment Organism Structure
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 Fd domain on HdrA and Fd Methanococcus maripaludis

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of His-tagged enzyme complex components, Fdh, Vhu, and Hdr in Escherichia coli Methanococcus maripaludis

Inhibitors

Inhibitors Comment Organism Structure
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 Methanococcus maripaludis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 formate + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB Methanococcus maripaludis
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 2 CO2 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?
2 formate + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB Methanococcus maripaludis LL
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 2 CO2 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?

Organism

Organism UniProt Comment Textmining
Methanococcus maripaludis
-
 and strains Mm1264 and Mm1265, derivatives of strain S2 incorporating a poly-His-tag at the C-terminus of HdrB (1264) and at the C-terminus of FdhA (1265), respectively
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Methanococcus maripaludis LL
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 and strains Mm1264 and Mm1265, derivatives of strain S2 incorporating a poly-His-tag at the C-terminus of HdrB (1264) and at the C-terminus of FdhA (1265), respectively
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme complex components, Fdh, Vhu, and Hdr from Escherichia coli by nickel affinity chromatography Methanococcus maripaludis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
36
-
 FBEB activity in presence of phosphate, pH 7.0, 30°C Methanococcus maripaludis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 formate + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
 Methanococcus maripaludis 2 CO2 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?
2 formate + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
 Methanococcus maripaludis LL 2 CO2 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
 ?
additional information in Escherichia coli recombinantly expressed Clostridium pasteurianum ferredoxin is used as cosubstrate. The Fdh containing complexes show higher activity with formate compared to hydrogen. The non-FBEB reduction of Fd by Vhu (H2 oxidation) or Fdh (formate oxidation) is not kinetically dominant Methanococcus maripaludis ?
-
-
additional information in Escherichia coli recombinantly expressed Clostridium pasteurianum ferredoxin is used as cosubstrate. The Fdh containing complexes show higher activity with formate compared to hydrogen. The non-FBEB reduction of Fd by Vhu (H2 oxidation) or Fdh (formate oxidation) is not kinetically dominant Methanococcus maripaludis LL ?
-
-

Subunits

Subunits Comment Organism
More 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) Methanococcus maripaludis

Synonyms

Synonyms Comment Organism
FDH
-
 Methanococcus maripaludis
formate-driven FBEB
-
 Methanococcus maripaludis
heterodisulfide reductase complex
-
 Methanococcus maripaludis
More see also EC 1.8.98.5 Methanococcus maripaludis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Methanococcus maripaludis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Methanococcus maripaludis

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Methanococcus maripaludis
Fe-S center two [4Fe-4S] clusters of the inserted ferredoxin (Fd) domain Methanococcus maripaludis
Ferredoxin
-
 Methanococcus maripaludis

General Information

General Information Comment Organism
metabolism heterodisulfide reductase plays a central role in the methanogenesis cycle of Methanococcus maripaludis. 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 Methanococcus maripaludis
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 Methanococcus maripaludis