EC - NADH:ubiquinone reductase (H+-translocating)

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IntEnz Enzyme Nomenclature


Accepted name:
NADH:ubiquinone reductase (H+-translocating)
Other names:
DPNH-coenzyme Q reductase [ambiguous]
DPNH-ubiquinone reductase [ambiguous]
NADH coenzyme Q1 reductase
NADH-CoQ oxidoreductase [ambiguous]
NADH-CoQ reductase [ambiguous]
NADH-Q6 oxidoreductase [ambiguous]
NADH-coenzyme Q oxidoreductase [ambiguous]
NADH-coenzyme Q reductase [ambiguous]
NADH-ubiquinone oxidoreductase [ambiguous]
NADH-ubiquinone reductase [ambiguous]
NADH-ubiquinone-1 reductase
NADH:ubiquinone oxidoreductase complex
coenzyme Q reductase [ambiguous]
complex 1 dehydrogenase
complex I (NADH:Q1 oxidoreductase)
complex I (electron transport chain)
complex I (mitochondrial electron transport)
dihydronicotinamide adenine dinucleotide-coenzyme Q reductase [ambiguous]
electron transfer complex I
mitochondrial electron transport complex 1
mitochondrial electron transport complex I
reduced nicotinamide adenine dinucleotide-coenzyme Q reductase [ambiguous]
type 1 dehydrogenase
ubiquinone reductase [ambiguous]
NADH dehydrogenase (ubiquinone)
Systematic name:
NADH:ubiquinone oxidoreductase




The enzyme is a very large complex that participates in electron transfer chains of mitochondria and aerobic bacteria. The mitochondrial enzyme transfers electrons from NADH to the ubiquinone pool. The cyanobacterial enzyme prefers NADPH, reduces plastoquinone, and also participates in reversed electron transport that results in the reduction of NAD(P)+ to NAD(P)H. Formerly EC

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00468 , PROSITE:PDOC00521 , PROSITE:PDOC00554 , PROSITE:PDOC00555 , PROSITE:PDOC00570 , PROSITE:PDOC00843 , PROSITE:PDOC00858
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008137
CAS Registry Number: 9028-04-0
UniProtKB/Swiss-Prot: (1000) [show] [UniProt]


  1. Hatefi, Y., Ragan, C.I. and Galante, Y.M.
    The enzymes and the enzyme complexs of the mitochondrial oxidative phosphorylation system.
    In: Martonosi, A.N. (Ed.) The Enzymes of Biological Membranes , 2nd ed. vol. 4 , Wiley , New York , 1985 , 1-70
  2. Herter, S. M., Kortluke, C. M., Drews, G.
    Complex I of Rhodobacter capsulatus and its role in reverted electron transport.
    Arch. Microbiol. 169 : 98-105 (1998). [PMID: 9446680]
  3. Hunte, C., Zickermann, V., Brandt, U.
    Functional modules and structural basis of conformational coupling in mitochondrial complex I.
    Science 329 : 448-451 (2010). [PMID: 20595580]
  4. Efremov, R. G., Baradaran, R., Sazanov, L. A.
    The architecture of respiratory complex I.
    Nature 465 : 441-445 (2010). [PMID: 20505720]
  5. Wikström, M., Hummer, G.
    Stoichiometry of proton translocation by respiratory complex I and its mechanistic implications.
    Proc. Natl. Acad. Sci. U.S.A. 109 : 4431-4436 (2012). [PMID: 22392981]

[EC created 1961 as EC, deleted 1965, reinstated 1983, modified 2011, modified 2013, transferred 2018 to EC]