Nitric oxide reductase (NAD(P), nitrous oxide-forming)
Appearance
Nitric oxide reductase (NAD(P), nitrous oxide-forming) | |||||||||
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Identifiers | |||||||||
EC no. | 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 2 NO + NAD(P)H + H+
This enzyme is heme-thiolate protein (P450).
References
- ^ Shoun H, Tanimoto T (June 1991). "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. PMID 2040619.
- ^ Shiro Y, Fujii M, Iizuka T, Adachi S, Tsukamoto K, Nakahara K, Shoun H (January 1995). "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. PMID 7829493.
- ^ Zhang L, Kudo T, Takaya N, Shoun H (September 2002). "The B' helix determines cytochrome P450nor specificity for the electron donors NADH and NADPH". The Journal of Biological Chemistry. 277 (37): 33842–7. doi:10.1074/jbc.M203923200. PMID 12105197.
- ^ Oshima R, Fushinobu S, Su F, Zhang L, Takaya N, Shoun H (September 2004). "Structural evidence for direct hydride transfer from NADH to cytochrome P450nor". Journal of Molecular Biology. 342 (1): 207–17. doi:10.1016/j.jmb.2004.07.009. PMID 15313618.
External links
- Nitric+oxide+reductase+(NAD(P),+nitrous+oxide-forming) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)