1.8.98.6: formate:CoB-CoM heterodisulfide,ferredoxin reductase
This is an abbreviated version!
For detailed information about formate:CoB-CoM heterodisulfide,ferredoxin reductase, go to the full flat file.
Reaction
2 CO2
+
2 reduced ferredoxin [iron-sulfur] cluster
+
Synonyms
FDH, FdhGHI, formate-driven FBEB, formate: CoMS-S-CoB oxidoreductase, HdrABC-VhuAUGD, HdrDE, HdrDE-FdhGHI, heterodisulfide reductase, heterodisulfide reductase complex, More
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1.8.98.6 formate:CoB-CoM heterodisulfide,ferredoxin reductaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.8.98.6 - formate:CoB-CoM heterodisulfide,ferredoxin 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 formate + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 CO2 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
CO2 + reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + H+
formate + oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
-
-
-
-
?
2 formate + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 CO2 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
-
?
2 formate + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 CO2 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
-
?
2 formate + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 CO2 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
?
2 formate + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 CO2 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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
-
-
?
2 formate + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 CO2 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
-
-
-
?
2 formate + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB
2 CO2 + 2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H+
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
-
-
?
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
-
-
?
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
-
-
-
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
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