EC - Nitric-oxide reductase (cytochrome c)

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IntEnz Enzyme Nomenclature


Accepted name:
nitric-oxide reductase (cytochrome c)
Systematic name:
nitrous oxide:ferricytochrome-c oxidoreductase




The enzyme from Pseudomonas aeruginosa contains a dinuclear centre comprising a non-heme iron centre and heme b3, plus heme c, heme b and calcium; the acceptor is cytochrome c551.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0016966


  1. Hendriks, J., Warne, A., Gohlke, U., Haltia, T., Ludovici, C., Lubben, M., Saraste, M.
    The active site of the bacterial nitric oxide reductase is a dinuclear iron center.
    Biochemistry 37 : 13102-13109 (1998). [PMID: 9748316]
  2. Hendriks, J., Gohlke, U., Saraste, M.
    From NO to OO: nitric oxide and dioxygen in bacterial respiration.
    J. Bioenerg. Biomembr. 30 : 15-24 (1998). [PMID: 9623801]
  3. Heiss, B., Frunzke, K., Zumft, W. G.
    Formation of the N-N bond from nitric oxide by a membrane-bound cytochrome bc complex of nitrate-respiring (denitrifying) Pseudomonas stutzeri.
    J. Bacteriol. 171 : 3288-3297 (1989). [PMID: 2542222]
  4. Cheesman, M. R., Zumft, W. G., Thomson, A. J.
    The MCD and EPR of the heme centers of nitric oxide reductase from Pseudomonas stutzeri: evidence that the enzyme is structurally related to the heme-copper oxidases.
    Biochemistry 37 : 3994-4000 (1998). [PMID: 9521721]
  5. Kumita, H., Matsuura, K., Hino, T., Takahashi, S., Hori, H., Fukumori, Y., Morishima, I., Shiro, Y.
    NO reduction by nitric-oxide reductase from denitrifying bacterium Pseudomonas aeruginosa: characterization of reaction intermediates that appear in the single turnover cycle.
    J. Biol. Chem. 279 : 55247-55254 (2004). [PMID: 15504726]
  6. Hino, T., Matsumoto, Y., Nagano, S., Sugimoto, H., Fukumori, Y., Murata, T., Iwata, S., Shiro, Y.
    Structural basis of biological N2O generation by bacterial nitric oxide reductase.
    Science 330 : 1666-1670 (2010). [PMID: 21109633]

[EC created 1992 as EC, transferred 2011 to EC]