Nitric oxide reductase (cytochrome c)
| Nitric oxide reductase (cytochrome c) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.7.2.5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Nitric oxide reductase (cytochrome c) (EC 1.7.2.5) is an enzyme with systematic name nitrous oxide:ferricytochrome-c oxidoreductase.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction
- nitrous oxide + 2 ferricytochrome c + H2O 2 nitric oxide + 2 ferrocytochrome c + 2 H+
The enzyme from Pseudomonas aeruginosa contains a dinuclear centre.
References
- ↑ Hendriks, J.; Warne, A.; Gohlke, U.; Haltia, T.; Ludovici, C.; Lubben, M.; Saraste, M. (1998). "The active site of the bacterial nitric oxide reductase is a dinuclear iron center". Biochemistry. 37: 13102–13109. doi:10.1021/bi980943x. PMID 9748316.
- ↑ Hendriks, J.; Gohlke, U.; Saraste, M. (1998). "From NO to OO: nitric oxide and dioxygen in bacterial respiration". J. Bioenerg. Biomembr. 30 (1): 15–24. doi:10.1023/A:1020547225398. PMID 9623801.
- ↑ Heiss, B.; Frunzke, K.; Zumpft, W.G. (1989). "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 (6): 3288–3297. PMC 210048
. PMID 2542222. - ↑ Cheesman, M.R.; Zumft, W.G.; Thomson, A.J. (1998). "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. doi:10.1021/bi972437y. PMID 9521721.
- ↑ Kumita, H.; Matsuura, K.; Hino, T.; Takahashi, S.; Hori, H.; Fukumori, Y.; Morishima, I.; Shiro, Y. (2004). "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. doi:10.1074/jbc.M409996200. PMID 15504726.
- ↑ Hino, T.; Matsumoto, Y.; Nagano, S.; Sugimoto, H.; Fukumori, Y.; Murata, T.; Iwata, S.; Shiro, Y. (2010). "Structural basis of biological N2O generation by bacterial nitric oxide reductase". Science. 330: 1666–1670. doi:10.1126/science.1195591. PMID 21109633.
External links
- Nitric oxide reductase (cytochrome c) at the US National Library of Medicine Medical Subject Headings (MeSH)
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