EC number:7.1.1.7
Enzyme
Download| EC Tree |
| 7. Translocases |
| 7.1 Catalysing the translocation of hydrons |
| 7.1.1 Linked to oxidoreductase reactions |
| ID: | 7.1.1.7 |
|---|---|
| Description: | Ubiquinol oxidase (electrogenic, proton-motive force generating). |
| Alternative Name: |
Cytochrome bd-I oxidase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 7.1.1.7 |
| BRENDA Enzyme Link: | BRENDA 7.1.1.7 |
| KEGG Enzyme Link: | KEGG7.1.1.7 |
| BioCyc Enzyme Link: | BioCyc 7.1.1.7 |
| ExPASy Enzyme Link: | ExPASy7.1.1.7 |
| EC2PDB Enzyme Link: | EC2PDB 7.1.1.7 |
| ExplorEnz Enzyme Link: | ExplorEnz 7.1.1.7 |
| PRIAM enzyme-specific profiles Link: | PRIAM 7.1.1.7 |
| IntEnz Enzyme Link: | IntEnz 7.1.1.7 |
| MEDLINE Enzyme Link: | MEDLINE 7.1.1.7 |
| RHEA:40527 | 2 a ubiquinol + 4 H(+)(in) + O2(in) = 2 a ubiquinone + 4 H(+)(out) + 2 H2O(in) |
| RULE(radius=1) | [*:1]-[c;H0;+0:2]1:[c;H0;+0:3](-[*:4]):[c;H0;+0:5](-[OH;+0:6]):[c;H0;+0:7](-[*:8]):[c;H0;+0:9](-[*:10]):[c;H0;+0:11]:1-[OH;+0:12].[*:13]-[c;H0;+0:14]1:[c;H0;+0:15](-[OH;+0:16]):[c;H0;+0:17](-[*:18]):[c;H0;+0:19](-[*:20]):[c;H0;+0:21](-[OH;+0:22]):[c;H0;+0:23]:1-[*:24].[O;H0;+0:25]=[O;H0;+0:26]>>[*:1]-[C;H0;+0:2]1=[C;H0;+0:3](-[*:4])-[C;H0;+0:5](=[O;H0;+0:6])-[C;H0;+0:7](-[*:8])=[C;H0;+0:9](-[*:10])-[C;H0;+0:11]-1=[O;H0;+0:12].[*:13]-[C;H0;+0:14]1=[C;H0;+0:23](-[*:24])-[C;H0;+0:21](=[O;H0;+0:22])-[C;H0;+0:19](-[*:20])=[C;H0;+0:17](-[*:18])-[C;H0;+0:15]-1=[O;H0;+0:16].[OH2;+0:25].[OH2;+0:26] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The active form of the cytochrome d terminal oxidase complex of Escherichia coli is a heterodimer containing one copy of each of the two subunits. | Miller MJ, Hermodson M, Gennis RB | 1988 Apr 15 | 3281937 |
| Clustering and dynamics of cytochrome bd-I complexes in the Escherichia coli plasma membrane in vivo. | Lenn T, Leake MC, Mullineaux CW | 2008 Dec | 19019148 |
| Properties of the two terminal oxidases of Escherichia coli. | Puustinen A, Finel M, Haltia T, Gennis RB, Wikström M | 1991 Apr 23 | 1850294 |
| Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site. | Belevich I, Borisov VB, Zhang J, Yang K, Konstantinov AA, Gennis RB, Verkhovsky MI | 2005 Mar 8 | 15728392 |