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EC 1.17.1.11 Details

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EC number

1.17.1.11

Accepted name

formate dehydrogenase (NAD⁺, ferredoxin)

Reaction

2 formate + NAD⁺ + 2 oxidized ferredoxin [iron-sulfur] cluster = 2 CO₂ + NADH + H⁺ + 2 reduced ferredoxin [iron-sulfur] cluster

Other name(s)

electron-bifurcating formate dehydrogenase

Systematic name

formate:NAD⁺, ferredoxin oxidoreductase

Comment

The enzyme complex, isolated from the bacterium Gottschalkia acidurici, couples the reduction of NAD⁺ and the reduction of ferredoxin with formate via flavin-based electron bifurcation.

History

created 2015 as EC 1.2.1.93, transferred 2017 to EC 1.17.1.11

EC Tree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.2 Acting on the aldehyde or oxo group of donors

1.3 Acting on the CH-CH group of donors

1.4 Acting on the CH-NH₂ group of donors

1.5 Acting on the CH-NH group of donors

1.6 Acting on NADH or NADPH

1.6.1 With NAD⁺ or NADP⁺ as acceptor

1.6.2 With a heme protein as acceptor

1.6.3 With oxygen as acceptor

1.6.4 With a disulfide as acceptor (deleted sub-subclass)

1.6.5 With a quinone or similar compound as acceptor

1.6.5.1 created 1961, deleted 1965

1.6.5.2 NAD(P)H dehydrogenase (quinone)

1.6.5.3 NADH:ubiquinone reductase (H⁺-translocating)

1.6.5.4 monodehydroascorbate reductase (NADH)

1.6.5.5 NADPH:quinone reductase

1.6.5.6 p-benzoquinone reductase (NADPH)

1.6.5.7 2-hydroxy-1,4-benzoquinone reductase

1.6.5.8 NADH:ubiquinone reductase (Na⁺-transporting)

1.6.5.9 NADH:quinone reductase (non-electrogenic)

1.6.5.10 NADPH dehydrogenase (quinone)

1.6.5.11 NADH dehydrogenase (quinone)

1.6.5.12 demethylphylloquinone reductase

1.6.6 With a nitrogenous group as acceptor

1.6.7 With an iron-sulfur protein as acceptor (deleted sub-subclass)

1.6.8 With a flavin as acceptor (deleted sub-subclass)

1.6.8.1 created 1981, deleted 2002

1.6.8.2 created 1982, deleted 2002

1.6.99 With unknown physiological acceptors

1.7 Acting on other nitrogenous compounds as donors

1.8 Acting on a sulfur group of donors

1.9 Acting on a heme group of donors

1.10 Acting on diphenols and related substances as donors

1.11 Acting on a peroxide as acceptor

1.12 Acting on hydrogen as donor

1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.15 Acting on superoxide as acceptor

1.16 Oxidizing metal ions

1.17 Acting on CH or CH₂ groups

1.17.1 With NAD⁺ or NADP⁺ as acceptor

1.17.1.1 CDP-4-dehydro-6-deoxyglucose reductase

1.17.1.2 4-hydroxy-3-methylbut-2-enyl diphosphate reductase

1.17.1.3 leucoanthocyanidin reductase

1.17.1.4 xanthine dehydrogenase

1.17.1.5 nicotinate dehydrogenase

1.17.1.6 bile-acid 7α-dehydroxylase

1.17.1.7 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase

1.17.1.8 4-hydroxy-tetrahydrodipicolinate reductase

1.17.1.9 formate dehydrogenase

1.17.1.10 formate dehydrogenase (NADP⁺)

1.17.1.11 formate dehydrogenase (NAD⁺, ferredoxin)

1.17.2 With a cytochrome as acceptor

1.17.3 With oxygen as acceptor

1.17.4 With a disulfide as acceptor

1.17.5 With a quinone or similar compound as acceptor

1.17.7 With an iron-sulfur protein as acceptor

1.17.8 With a flavin as acceptor

1.17.9 With a copper protein as acceptor

1.17.98 With other, known, physiological acceptors

1.17.99 With unknown physiological acceptors

1.18 Acting on iron-sulfur proteins as donors

1.19 Acting on reduced flavodoxin as donor

1.20 Acting on phosphorus or arsenic in donors

1.20.1 With NAD⁺ or NADP⁺ as acceptor

1.20.2 With a cytochrome as acceptor

1.20.4 With disulfide as acceptor

1.20.9 With a copper protein as acceptor

1.20.98 With other, known, physiological acceptors

1.20.99 With unknown physiological acceptors

1.21 Catalysing the reaction X-H + Y-H = X-Y

1.22 Acting on halogen in donors

1.23 Reducing C-O-C group as acceptor

1.97 Other oxidoreductases

1.98 Enzymes using H₂ as reductant (deleted subclass)

1.99 Other enzymes using O₂ as oxidant (deleted subclass)

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Release 2023.1 (January 2023)