Application | Comment | Organism |
---|---|---|
additional information | the monomeric form of Rhodobacter sphaeroides COX when reconstituted into a phospholipid bilayer is completely functionally active in its ability to perform electron transfer and proton pumping activities of the enzyme | Cereibacter sphaeroides |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | - |
Cereibacter sphaeroides | 5739 | - |
additional information | cytochrome oxidase unilamellar vesicles (COV). Purified COV contains approximately 1 COX molecule per liposome. Purified COV exhibits similar physical properties as unpurified COV | Cereibacter sphaeroides | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Cereibacter sphaeroides | - |
- |
- |
Purification (Comment) | Organism |
---|---|
polyhistidine-labeled protein purified on a Ni-NTA column | Cereibacter sphaeroides |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ferrocytochrome c + O2 + H+ | - |
Cereibacter sphaeroides | ferricytochrome c + H2O | - |
r | |
reduced cytochrome c + O2 + H+ | - |
Cereibacter sphaeroides | oxidized cytochrome c + H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | - |
Cereibacter sphaeroides |
Synonyms | Comment | Organism |
---|---|---|
COX | - |
Cereibacter sphaeroides |
cytochrome c oxidase | - |
Cereibacter sphaeroides |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
535 | - |
ferrocytochrome c | purified COV | Cereibacter sphaeroides | |
708 | - |
ferrocytochrome c | unpurified COV | Cereibacter sphaeroides |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | heme aa3 | Cereibacter sphaeroides |