EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
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 | - |
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EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.8.98.6 | Methanococcus maripaludis | - |
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EC Number | Purification (Comment) | Organism |
---|---|---|
1.8.98.6 | Ni2+ resin column chromatography | Methanococcus maripaludis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
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 | - |
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1.8.98.6 | additional information | 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 | ? | - |
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