| Entry |
|
| Name |
nitric oxide reductase [NAD(P)+, nitrous oxide-forming];
fungal nitric oxide reductase;
cytochrome P450nor;
NOR (ambiguous)
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| Class |
Oxidoreductases;
Acting on other nitrogenous compounds as donors;
With NAD+ or NADP+ as acceptor
 |
| Sysname |
nitrous oxide:NAD(P) oxidoreductase
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| Reaction(IUBMB) |
N2O + NAD(P)+ + H2O = 2 NO + NAD(P)H + H+ [RN: R02492 R09446]
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| Reaction(KEGG) |
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| Substrate |
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| Product |
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| Comment |
A heme-thiolate protein (P-450). The enzyme from Fusarium oxysporum utilizes only NADH, but the isozyme from Trichosporon cutaneum utilizes both NADH and NADPH. The electron transfer from NAD(P)H to heme occurs directly, not requiring flavin or other redox cofactors.
|
| Pathway |
| Nitrogen metabolism | | Microbial metabolism in diverse environments |
|
| Orthology |
| fungal nitric oxide reductase |
|
| Genes |
NCR: | | SMP: | | PAN: | | NHE: | | SSL: | | AOR: | | ANG: | | AFV: | | URE: | | ABE: | | TVE: | | » show all
 |
| Reference |
|
| Authors |
Shoun H, Tanimoto T |
| Title |
Denitrification by the fungus Fusarium oxysporum and involvement of cytochrome P-450 in the respiratory nitrite reduction. |
| Journal |
J. Biol. Chem. 266 (1991) 11078-82. |
| Reference |
|
| Authors |
Shiro Y, Fujii M, Iizuka T, Adachi S, Tsukamoto K, Nakahara K, Shoun H |
| Title |
Spectroscopic and kinetic studies on reaction of cytochrome P450nor with nitric oxide. Implication for its nitric oxide reduction mechanism. |
| Journal |
J. Biol. Chem. 270 (1995) 1617-23. |
| Reference |
|
| Authors |
Zhang L, Kudo T, Takaya N, Shoun H |
| Title |
The B' helix determines cytochrome P450nor specificity for the electron donors NADH and NADPH. |
| Journal |
J. Biol. Chem. 277 (2002) 33842-7. |
| Reference |
|
| Authors |
Oshima R, Fushinobu S, Su F, Zhang L, Takaya N, Shoun H |
| Title |
Structural evidence for direct hydride transfer from NADH to cytochrome P450nor. |
| Journal |
J. Mol. Biol. 342 (2004) 207-17. |
| Other DBs |
ExplorEnz - The Enzyme Database: IUBMB Enzyme Nomenclature: ExPASy - ENZYME nomenclature database: BRENDA, the Enzyme Database: |