NADH_dehydrogenase

NADH dehydrogenase

NADH dehydrogenase

Enzyme

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
Quick Facts Identifiers, EC no. ...

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 1.6.5.11) is defined for NADH dehydrogenases that use a quinone (excluding ubiquinone) as the acceptor. The EC term NADH dehydrogenase (ubiquinone) (EC 7.1.1.2) is defined for those with ubiquinone as the acceptor.

References

  1. [1]
    EC 1.6.99.3
  2. [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. [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. [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. [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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