| Nitric oxide reductase (cytochrome c) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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
- 2 nitric oxide + 2 ferrocytochrome c + 2 H+ nitrous oxide + 2 ferricytochrome c + H2O
The enzyme from Pseudomonas aeruginosa contains a dinuclear centre.
References
- ↑ Hendriks J, Warne A, Gohlke U, Haltia T, Ludovici C, Lübben M, Saraste M (September 1998). "The active site of the bacterial nitric oxide reductase is a dinuclear iron center". Biochemistry. 37 (38): 13102–9. doi:10.1021/bi980943x. PMID 9748316.
- ↑ Hendriks J, Gohlke U, Saraste M (February 1998). "From NO to OO: nitric oxide and dioxygen in bacterial respiration". Journal of Bioenergetics and Biomembranes. 30 (1): 15–24. doi:10.1023/A:1020547225398. PMID 9623801.
- ↑ Heiss B, Frunzke K, Zumft WG (June 1989). "Formation of the N-N bond from nitric oxide by a membrane-bound cytochrome bc complex of nitrate-respiring (denitrifying) Pseudomonas stutzeri". Journal of Bacteriology. 171 (6): 3288–97. PMC 210048. PMID 2542222.
- ↑ Cheesman MR, Zumft WG, Thomson AJ (March 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 (11): 3994–4000. doi:10.1021/bi972437y. PMID 9521721.
- ↑ Kumita H, Matsuura K, Hino T, Takahashi S, Hori H, Fukumori Y, Morishima I, Shiro Y (December 2004). "NO reduction by nitric-oxide reductase from denitrifying bacterium Pseudomonas aeruginosa: characterization of reaction intermediates that appear in the single turnover cycle". The Journal of Biological Chemistry. 279 (53): 55247–54. doi:10.1074/jbc.M409996200. PMID 15504726.
- ↑ Hino T, Matsumoto Y, Nagano S, Sugimoto H, Fukumori Y, Murata T, Iwata S, Shiro Y (December 2010). "Structural basis of biological N2O generation by bacterial nitric oxide reductase". Science. 330 (6011): 1666–70. doi:10.1126/science.1195591. PMID 21109633.
External links
- Nitric+oxide+reductase+(cytochrome+c) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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