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In enzymology, a rubredoxin-NAD reductase (EC 1.18.1.1) is an enzyme that catalyzes the chemical reaction.

2 reduced rubredoxin + NAD + H ${\displaystyle \rightleftharpoons }$ 2 oxidized rubredoxin + NADH

The 3 substrates of this enzyme are reduced rubredoxin, NAD, and H, whereas its two products are oxidized rubredoxin and NADH.

This enzyme belongs to the family of oxidoreductases, specifically those acting on iron-sulfur proteins as donor with NAD or NADP as acceptor. The systematic name of this enzyme class is rubredoxin:NAD oxidoreductase. Other names in common use include rubredoxin reductase, rubredoxin-nicotinamide adenine dinucleotide reductase, dihydronicotinamide adenine dinucleotide-rubredoxin reductase, reduced nicotinamide adenine dinucleotide-rubredoxin reductase, NADH-rubredoxin reductase, rubredoxin-NAD reductase, NADH: rubredoxin oxidoreductase, DPNH-rubredoxin reductase, and NADH-rubredoxin oxidoreductase. This enzyme participates in fatty acid metabolism. It has 2 cofactors: FAD and Iron.

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1BFY.

See also

• Rubredoxin—NAD(P)(+) reductase

References

• Peterson JA, Kusunose M, Kusunose E, Coon MJ (1967). "Enzymatic omega-oxidation. II. Function of rubredoxin as the electron carrier in omega-hydroxylation". J. Biol. Chem. 242 (19): 4334–40. doi:10.1016/S0021-9258(18)99543-8. PMID 4294330.
• "Enzymatic -oxidation. VI. Isolation of homogeneous reduced diphosphopyridine nucleotide-rubredoxin reductase". J. Biol. Chem. 247 (7): 2109–16. 1972. PMID 4335861.
• Ueda T, Coon MJ (1972). "Enzymatic oxidation. VII. Reduced diphosphopyridine nucleotide-rubredoxin reductase: properties and function as an electron carrier in hydroxylation". J. Biol. Chem. 247 (16): 5010–6. doi:10.1016/S0021-9258(19)44932-6. PMID 4403503.
• Petitdemange H, Marczak R, Blusson H, Gay R (1979). "Isolation and properties of reduced nicotinamide adenine dinucleotiderubredoxin oxidoreductase of Clostridium acetobutylicum". Biochem. Biophys. Res. Commun. 91 (4): 1258–65. doi:10.1016/0006-291X(79)91202-6. PMID 526302.

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