| EC Tree |
| 1. Oxidoreductases |
| 1.7 Acting on other nitrogenous compounds as donors |
| 1.7.5 With a quinone or similar compound as acceptor |
| ID: | 1.7.5.2 |
|---|---|
| Description: | Nitric oxide reductase (menaquinol). |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| UniProtKB Enzyme Link: | UniProtKB 1.7.5.2 |
| BRENDA Enzyme Link: | BRENDA 1.7.5.2 |
| KEGG Enzyme Link: | KEGG1.7.5.2 |
| BioCyc Enzyme Link: | BioCyc 1.7.5.2 |
| ExPASy Enzyme Link: | ExPASy1.7.5.2 |
| EC2PDB Enzyme Link: | EC2PDB 1.7.5.2 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.7.5.2 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.7.5.2 |
| IntEnz Enzyme Link: | IntEnz 1.7.5.2 |
| MEDLINE Enzyme Link: | MEDLINE 1.7.5.2 |
| RHEA:30215 | a menaquinol + 2 nitric oxide = a menaquinone + H2O + nitrous oxide |
| RULE(radius=1) | [*:1]:[cH;+0:2]:[*:3]1:[c;H0;+0:4](-[OH;+0:5]):[cH;+0:6]:[c;H0;+0:7](-[*:8]):[c;H0;+0:9](-[OH;+0:10]):[c;H0;+0:11]:1:[*:12].[NH;+0:13]=[O;H0;+0:14].[NH;+0:15]=[O;H0;+0:16]>>[*:1]:[c;H0;+0:2]1:[*:3](:[cH;+0:11]:[*:12])-[C;H0;+0:4](=[O;H0;+0:5])-[CH;+0:6]=[C;H0;+0:7](-[*:8])-[C;H0;+0:9]-1=[O;H0;+0:10].[N;H0;+0:15]#[N+;H0:13]-[OH;+0:14].[OH2;+0:16] |
| Reaction | ![]() |
| Core-to-Core |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| NO reductase from Bacillus azotoformans is a bifunctional enzyme accepting electrons from menaquinol and a specific endogenous membrane-bound cytochrome c551. | Suharti, Heering HA, de Vries S | 2004 Oct 26 | 15491156 |
| A novel copper A containing menaquinol NO reductase from Bacillus azotoformans. | Suharti, Strampraad MJ, Schröder I, de Vries S | 2001 Feb 27 | 11327887 |
| Purification and characterization of the single-component nitric oxide reductase from Ralstonia eutropha H16. | Cramm R, Pohlmann A, Friedrich B | 1999 Oct 22 | 10571051 |