Biology:Nitric oxide reductase (NAD(P), nitrous oxide-forming)
From HandWiki
| Nitric oxide reductase (NAD(P), nitrous oxide-forming) | |||||||||
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| Identifiers | |||||||||
| EC number | 1.7.1.14 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Nitric oxide reductase (NAD(P), nitrous oxide-forming) (EC 1.7.1.14, fungal nitric oxide reductase, cytochrome P450nor, NOR (ambiguous)) is an enzyme with systematic name nitrous oxide:NAD(P) oxidoreductase.[1][2][3][4] This enzyme catalyses the following chemical reaction
- N2O + NAD(P)+ + H2O [math]\displaystyle{ \rightleftharpoons }[/math] 2 NO + NAD(P)H + H+
This enzyme is heme-thiolate protein (P450).
References
- ↑ "Denitrification by the fungus Fusarium oxysporum and involvement of cytochrome P-450 in the respiratory nitrite reduction". The Journal of Biological Chemistry 266 (17): 11078–82. June 1991. PMID 2040619.
- ↑ "Spectroscopic and kinetic studies on reaction of cytochrome P450nor with nitric oxide. Implication for its nitric oxide reduction mechanism". The Journal of Biological Chemistry 270 (4): 1617–23. January 1995. PMID 7829493.
- ↑ "The B' helix determines cytochrome P450nor specificity for the electron donors NADH and NADPH". The Journal of Biological Chemistry 277 (37): 33842–7. September 2002. doi:10.1074/jbc.M203923200. PMID 12105197.
- ↑ "Structural evidence for direct hydride transfer from NADH to cytochrome P450nor". Journal of Molecular Biology 342 (1): 207–17. September 2004. doi:10.1016/j.jmb.2004.07.009. PMID 15313618.
External links
- Nitric+oxide+reductase+(NAD(P),+nitrous+oxide-forming) at the US National Library of Medicine Medical Subject Headings (MeSH)
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