EC 1.6.5.3 - NADH:ubiquinone reductase (H+-translocating)

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IntEnz Enzyme Nomenclature
EC 1.6.5.3

Names

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

Reaction

Cofactors

Comments:

A flavoprotein (FMN) containing iron-sulfur clusters. The complex is present in mitochondria and aerobic bacteria. Breakdown of the complex can release EC 1.6.99.3, NADH dehydrogenase. In photosynthetic bacteria, reversed electron transport through this enzyme can reduce NAD+ to NADH.

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: (1377) [show] [UniProt]

References

  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 1.6.5.3 created 1961, deleted 1965, reinstated 1983, modified 2011]