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NADH dehydrogenase

This article may require cleanup to meet Wikipedia's quality standards. The specific problem is: Need to explain the deletion of EC due to being "covered by EC" (the ubiquinone one). Such a merge makes sense for some proteins tagged with that EC, but definitely does not make sense for this article. Please help improve this article if you can. (April 2022) (Learn how and when to remove this message)
NADH dehydrogenase
EC no.
CAS no.9079-67-8
Alt. namescytochrome c reductase, type 1 dehydrogenase, beta-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[1]
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum

NADH dehydrogenase is an enzyme that converts nicotinamide adenine dinucleotide (NAD) from its reduced form (NADH) to its oxidized form (NAD+). Members of the NADH dehydrogenase family and analogues are commonly systematically named using the format NADH:acceptor oxidoreductase.[2][3][4][5] The chemical reaction these enzymes catalyze is generally represented with the following equation:

NADH + H+ + acceptor ⇌ NAD+ + reduced acceptor

NADH dehydrogenase is a flavoprotein that contains iron-sulfur centers.

NADH dehydrogenase is used in the electron transport chain for generation of ATP.

The EC term NADH dehydrogenase (quinone) (EC is defined for NADH dehydrogenases that use a quinone (excluding ubiquinone) as the acceptor. The EC term NADH dehydrogenase (ubiquinone) (EC is defined for those with ubiquinone as the acceptor.


  1. ^ EC
  2. ^ Adachi K, Okuyama T (June 1972). "Study on the reduced pyridine nucleotide dehydrogenase of bovine erythrocytes. I. Crystallization and properties of the reduced pyridine nucleotide dehydrogenase of bovine erythrocytes". Biochimica et Biophysica Acta (BBA) - Enzymology. 268 (3): 629–37. doi:10.1016/0005-2744(72)90266-5. PMID 4402556.
  3. ^ Hatefi, Y.; Ragan, C.I.; Galante, Y.M. (1985). "The enzymes and the enzyme complexes of the mitochondrial oxidative phosphorylation system". In Martonosi, A. (ed.). The Enzymes of Biological Membranes. Vol. 4 (2nd ed.). New York: Plenum Press. pp. 1–70.
  4. ^ Hochstein LI, Dalton BP (April 1973). "Studies of a halophilic NADH dehydrogenase. I. Purification and properties of the enzyme". Biochimica et Biophysica Acta (BBA) - Enzymology. 302 (2): 216–28. doi:10.1016/0005-2744(73)90150-2. PMID 4144655.
  5. ^ Kaniuga Z (August 1963). "The transformation of mitochondrial NADH dehydrogenase into NADH: Cytochrome c oxidoreductase". Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects. 73 (4): 550–64. doi:10.1016/0926-6569(63)90175-5. PMID 14074130.
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NADH dehydrogenase
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