EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   1.8.98.6 | 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+ |
- |
? |
| 1.8.98.6 | 2 formate + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB |
- |
Methanonatronarchaeum thermophilum |
2 CO2 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ |
- |
? |
| 1.8.98.6 | 2 formate + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB |
electron flow occurs from formate 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 |
Methanonatronarchaeum thermophilum |
2 CO2 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ |
- |
? |
| 1.8.98.6 | 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+ |
- |
? |
| 1.8.98.6 | 2 formate + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB |
- |
Methanonatronarchaeum thermophilum AMET1 |
2 CO2 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ |
- |
? |
| 1.8.98.6 | 2 formate + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB |
electron flow occurs from formate 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 |
Methanonatronarchaeum thermophilum AMET1 |
2 CO2 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+ |
- |
? |
| 1.8.98.6 | CO2 + reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+ |
- |
Methanococcus maripaludis |
formate + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB |
- |
? |
| 1.8.98.6 | more |
the protein complex consists of heterodisulfide reductase, formylmethanofuran dehydrogenase, F420-nonreducing hydrogenase, and formate dehydrogenase. Either H2 or formate can donate electrons to the heterodisulfide-H2 via F420-nonreducing hydrogenase or formate via formate dehydrogenase. When H2 is used as the electron donor for methanogenesis, electrons are transferred to heterodisulfide reductase via F420-nonreducing hydrogenase. Flavin-mediated electron bifurcation at heterodisulfide reductase A then results in reduction of the CoM-S-S-CoB heterodisulfide and a ferredoxin that is used by formylmethanofuran dehydrogenase for the first step in methanogenesis. When hydrogen is limiting or is replaced by formate, formate dehydrogenase is highly expressed and incorporates into the complex. When formate is used as the electron donor for methanogenesis, electrons are transferred to heterodisulfide reductase from formate via formate dehydrogenase |
Methanococcus maripaludis |
? |
- |
? |
| 1.8.98.6 | more |
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 |
? |
- |
- |
| 1.8.98.6 | more |
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 |
? |
- |
- |
