ExplorEnz: EC 1.7.2.5

Your query returned 1 entry. Printable version

1.7.2.5

Accepted name:

nitric oxide reductase (cytochrome c)

Reaction:

nitrous oxide + 2 ferricytochrome c + H₂O = 2 nitric oxide + 2 ferrocytochrome c + 2 H⁺

Systematic name:

nitrous oxide:ferricytochrome-c oxidoreductase

Comments:

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:

BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Hendriks, J., Warne, A., Gohlke, U., Haltia, T., Ludovici, C., Lubben, M. and Saraste, M. The active site of the bacterial nitric oxide reductase is a dinuclear iron center. Biochemistry 37 (1998) 13102–13109. [DOI] [PMID: 9748316]
2.	Hendriks, J., Gohlke, U. and Saraste, M. From NO to OO: nitric oxide and dioxygen in bacterial respiration. J. Bioenerg. Biomembr. 30 (1998) 15–24. [PMID: 9623801]
3.	Heiss, B., Frunzke, K. and Zumpft, 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 (1989) 3288–3297. [DOI] [PMID: 2542222]
4.	Cheesman, M.R., Zumft, W.G. and 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 (1998) 3994–4000. [DOI] [PMID: 9521721]
5.	Kumita, H., Matsuura, K., Hino, T., Takahashi, S., Hori, H., Fukumori, Y., Morishima, I. and 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 (2004) 55247–55254. [DOI] [PMID: 15504726]
6.	Hino, T., Matsumoto, Y., Nagano, S., Sugimoto, H., Fukumori, Y., Murata, T., Iwata, S. and Shiro, Y. Structural basis of biological N₂O generation by bacterial nitric oxide reductase. Science 330 (2010) 1666–1670. [DOI] [PMID: 21109633]

[EC 1.7.2.5 created 1992 as EC 1.7.99.7, transferred 2011 to EC 1.7.2.5]