EC - NADH:ubiquinone reductase (Na+-transporting)

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IntEnz Enzyme Nomenclature


Accepted name:
NADH:ubiquinone reductase (Na+-transporting)
Other names:
Na+-translocating NADH-quinone reductase
Systematic name:
NADH:ubiquinone oxidoreductase (Na+-translocating)




An iron-sulfur flavoprotein, containing two covalently bound molecules of FMN, one noncovalently bound FAD, one riboflavin, and one [2Fe-2S] cluster. Formerly EC

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (327) [show] [UniProt]


  1. Beattie, P., Tan, K., Bourne, R. M., Leach, D., Rich, P. R., Ward, F. B.
    Cloning and sequencing of four structural genes for the Na+-translocating NADH-ubiquinone oxidoreductase of Vibrio alginolyticus.
    FEBS Lett. 356 : 333-338 (1994). [PMID: 7805867]
  2. Nakayama, Y., Hayashi, M., Unemoto, T.
    Identification of six subunits constituting Na+ -translocating NADH-quinone reductase from the marine Vibrio alginolyticus.
    FEBS Lett. 422 : 240-242 (1998). [PMID: 9490015]
  3. Bogachev, A. V., Bertsova, Y. V., Barquera, B., Verkhovsky, M. I.
    Sodium-dependent steps in the redox reactions of the Na+-motive NADH:quinone oxidoreductase from Vibrio harveyi.
    Biochemistry 40 : 7318-7323 (2001). [PMID: 11401580]
  4. Barquera, B., Hellwig, P., Zhou, W., Morgan, J. E., Hase, C. C., Gosink, K. K., Nilges, M., Bruesehoff, P. J., Roth, A., Lancaster, C. R., Gennis, R. B.
    Purification and characterization of the recombinant Na+-translocating NADH:quinone oxidoreductase from Vibrio cholerae.
    Biochemistry 41 : 3781-3789 (2002). [PMID: 11888296]
  5. Barquera, B., Nilges, M. J., Morgan, J. E., Ramirez-Silva, L., Zhou, W., Gennis, R. B.
    Mutagenesis study of the 2Fe-2S center and the FAD binding site of the Na+-translocating NADH:ubiquinone oxidoreductase from Vibrio cholerae.
    Biochemistry 43 : 12322-12330 (2004). [PMID: 15379571]

[EC created 2011 as EC, transferred 2018 to EC]