Reaction: NADH + H+ + acceptor = NAD+ + reduced acceptor
Other name(s): cytochrome c reductase; type 1 dehydrogenase; β-NADH dehydrogenase dinucleotide; diaphorase; dihydrocodehydrogenase I dehydrogenase; dihydronicotinamide adenine dinucleotide dehydrogenase; diphosphopyridine diaphorase; DPNH diaphorase; NADH diaphorase; NADH hydrogenase; NADH oxidoreductase; NADH-menadione oxidoreductase; reduced diphosphopyridine nucleotide diaphorase; NADH:cytochrome c oxidoreductase; NADH2 dehydrogenase; NADH:(acceptor) oxidoreductase
Systematic name: NADH:acceptor oxidoreductase
Comments: A flavoprotein containing iron-sulfur centres. After preparations have been subjected to certain treatments, cytochrome c may act as an acceptor. Under normal conditions, two protons are extruded from the cytoplasm or the intramitochondrial or stromal compartment. Present in a mitochondrial complex as EC 188.8.131.52, NADH:ubiquinone reductase (H+-translocating).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9079-67-8
1. Adachi, K. and Okuyama, T. Study on the reduced pyridine nucleotide dehydrogenase of bovine erythrocytes. I. Crystallization and properties of the reduced pyridine nucleotide dehydrogenase of bovine erythrocytes. Biochim. Biophys. Acta 268 (1972) 629-637. [PMID: 4402556]
2. Hatefi, Y., Ragan, C.I. and Galante, Y.M. The enzymes and the enzyme complexes of the mitochondrial oxidative phosphorylation system. In: Martonosi, A. (Ed.), The Enzymes of Biological Membranes, 2nd edn, vol. 4, Plenum Press, New York, 1985, pp. 1-70.
3. Hochstein, L.I. and Dalton, B.P. Studies of a halophilic NADH dehydrogenase. I. Purification and properties of the enzyme. Biochim. Biophys. Acta 302 (1973) 216-228. [PMID: 4144655]
4. Kaniuga, Z. The transformation of mitochondrial NADH dehydrogenase into NADH:Cytochrome c oxidoreductase. Biochim. Biophys. Acta 73 (1963) 550-564. [PMID: 14074130]