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formate dehydrogenase (NAD+) activity

Known as: formate dehydrogenase (NAD), formate-NAD oxidoreductase, NAD-dependent formate dehydrogenase 
Catalysis of the reaction: formate + NAD(+) = CO(2) + NADH. [EC:1.2.1.2, RHEA:15988]
National Institutes of Health

Related topics

Related topics

2 relations
Formate dehydrogenaseformate hydrogenlyase

Papers overview

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Highly Cited
2009
Highly Cited
2009
Hydrothermal Focusing of Chemical and Chemiosmotic Energy, Supported by Delivery of Catalytic Fe, Ni, Mo/W, Co, S and Se, Forced Life to Emerge
Energised by the protonmotive force and with the intervention of inorganic catalysts, at base Life reacts hydrogen from a variety… Expand
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Highly Cited
2002
Highly Cited
2002
Metabolic engineering of Escherichia coli: increase of NADH availability by overexpressing an NAD(+)-dependent formate dehydrogenase.
Metabolic engineering studies have generally focused on manipulating enzyme levels through either the amplification, addition, or… Expand
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Highly Cited
1997
Highly Cited
1997
A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system.
The nucleotide sequence has been determined for a twelve-gene operon of Escherichia coli designated the hyf operon (hyfABCDEFGHIR… Expand
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Highly Cited
1995
Highly Cited
1995
Genetic analysis of the modABCD (molybdate transport) operon of Escherichia coli.
DNA sequence analysis of the modABCD operon of Escherichia coli revealed the presence of four open reading frames. The first gene… Expand
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Highly Cited
1992
Highly Cited
1992
Mutational analysis of the operon (hyc) determining hydrogenase 3 formation in Escherichia coli
In‐frame deletions were introduced into each of the eight genes of the hyc operon coding for products required for the formation… Expand
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Highly Cited
1987
Highly Cited
1987
Cotranslational insertion of selenocysteine into formate dehydrogenase from Escherichia coli directed by a UGA codon.
The structural gene (fdhF) for the 80-kDa selenopolypeptide of formate dehydrogenase (formate:benzyl viologen oxidoreductase, EC… Expand
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Highly Cited
1987
Highly Cited
1987
The ability of scavengers to distinguish OH. production in the iron-catalyzed Haber-Weiss reaction: comparison of four assays for OH.
Kinetic analysis has been used to access how well scavenger inhibition can characterize the reactivity of oxidants produced in… Expand
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Highly Cited
1985
Highly Cited
1985
Differential expression of hydrogenase isoenzymes in Escherichia coli K-12: evidence for a third isoenzyme.
The cellular contents of the nickel-containing, membrane-bound hydrogenase isoenzymes 1 and 2 (hydrogenases 1 and 2) were… Expand
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Highly Cited
1979
Highly Cited
1979
Insulin-stimulated intracellular hydrogen peroxide production in rat epididymal fat cells.
Insulin stimulation of hydrogen peroxide production by rat epididymal fat cells was investigated by studying the oxidation of… Expand
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Highly Cited
1977
Highly Cited
1977
Role of quinones in electron transport to oxygen and nitrate in Escherichia coli. Studies with a ubiA- menA- double quinone mutant.
A ubiA- menA- double quinone mutant of Escherichia coli K12 was constructed together with other isogenic strains lacking either… Expand
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