Jump to content

Nitric oxide reductase (NAD(P), nitrous oxide-forming)

From Wikipedia, the free encyclopedia

This is an old revision of this page, as edited by OAbot (talk | contribs) at 03:26, 15 April 2020 (Open access bot: doi added to citation with #oabot.). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

Nitric oxide reductase (NAD(P), nitrous oxide-forming)
Identifiers
EC no.1.7.1.14
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

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

  1. ^ 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.
  2. ^ 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.
  3. ^ 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.
  4. ^ 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.