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Literature summary extracted from
- Reaction mechanism of superoxide generation during ubiquinol oxidation by the cytochrome bc1 complex (2010), J. Biol. Chem., 285, 17038-17045.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.1.1.8 | asolectin | stimulates superoxide anion production, overview | Bos taurus | |
| 7.1.1.8 | asolectin | stimulates superoxide anion production, overview | Cereibacter sphaeroides | |
| 7.1.1.8 | additional information | detergents stimulate superoxide anion production, overview | Bos taurus | |
| 7.1.1.8 | additional information | detergents stimulates superoxide anion production, overview | Cereibacter sphaeroides |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 7.1.1.8 | additional information | when the only supernumerary subunit (subunit IV) is deleted from the Rhodobaacter sphaeroides wild-type complex, the resulting three-subunit core complex has only a fraction of the electron transfer activity of the wild-type complex but has about four times the superoxide anions generating activity. When the three-subunit core complex is reconstituted with subunit IV, the electron transfer activity increases, and the O2 -.-generating activity decreases to the same level as those in the wild-type, four-subunit complex | Cereibacter sphaeroides |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.1.1.8 | antimycin A | - |
Bos taurus |  |
| 7.1.1.8 | antimycin A | - |
Cereibacter sphaeroides | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 7.1.1.8 | membrane | - |
Cereibacter sphaeroides | 16020 | - |
| 7.1.1.8 | mitochondrion | - |
Bos taurus | 5739 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.1.1.8 | Fe2+ | Rieske iron-sulfur protein | Cereibacter sphaeroides | |
| 7.1.1.8 | Fe2+ | Rieske ironsulfur protein | Bos taurus | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.1.1.8 | additional information | Cereibacter sphaeroides | reaction mechanism of superoxide generation by bc1, overview | ? | - |
? | |
| 7.1.1.8 | additional information | Bos taurus | reaction mechanism of superoxide generation by bc1, overview. Maximum superoxide anions generation activity is observed when the complex is inhibited by antimycin A or inactivated by heat treatment or proteinase K digestion. The protein subunits, at least those surrounding the QP pocket, may play a role either in preventing the release of superoxide. from its production site to aqueous environments or in preventing O2 from getting access to the hydrophobic QP pocket and might not directly participate in superoxide production | ? | - |
? | |
| 7.1.1.8 | quinol + 2 ferricytochrome c | Bos taurus | - |
quinone + 2 ferrocytochrome c + 2 H+ | - |
? | |
| 7.1.1.8 | quinol + 2 ferricytochrome c | Cereibacter sphaeroides | - |
quinone + 2 ferrocytochrome c + 2 H+ | - |
? | |
| 7.1.1.8 | ubiquinol + 2 ferricytochrome c | Bos taurus | - |
ubiquinone + 2 ferrocytochrome c + 2 H+ | - |
? | |
| 7.1.1.8 | ubiquinol + 2 ferricytochrome c | Cereibacter sphaeroides | - |
ubiquinone + 2 ferrocytochrome c + 2 H+ | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 7.1.1.8 | Bos taurus | - |
- |
- |
| 7.1.1.8 | Cereibacter sphaeroides | - |
- |
- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 7.1.1.8 | quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2] | reaction mechanism of superoxide generation during ubiquinol oxidation by the cytochrome bc1 complex | Bos taurus | |
| 7.1.1.8 | quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2] | reaction mechanism of superoxide generation during ubiquinol oxidation by the cytochrome bc1 complex | Cereibacter sphaeroides |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 7.1.1.8 | heart | - |
Bos taurus | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.1.1.8 | additional information | reaction mechanism of superoxide generation by bc1, overview | Cereibacter sphaeroides | ? | - |
? | |
| 7.1.1.8 | additional information | reaction mechanism of superoxide generation by bc1, overview. Maximum superoxide anions generation activity is observed when the complex is inhibited by antimycin A or inactivated by heat treatment or proteinase K digestion. The protein subunits, at least those surrounding the QP pocket, may play a role either in preventing the release of superoxide. from its production site to aqueous environments or in preventing O2 from getting access to the hydrophobic QP pocket and might not directly participate in superoxide production | Bos taurus | ? | - |
? | |
| 7.1.1.8 | quinol + 2 ferricytochrome c | - |
Bos taurus | quinone + 2 ferrocytochrome c + 2 H+ | - |
? | |
| 7.1.1.8 | quinol + 2 ferricytochrome c | - |
Cereibacter sphaeroides | quinone + 2 ferrocytochrome c + 2 H+ | - |
? | |
| 7.1.1.8 | ubiquinol + 2 ferricyanide | - |
Bos taurus | ubiquinone + 2 ferrocyanide + 2 H+ | - |
? | |
| 7.1.1.8 | ubiquinol + 2 ferricyanide | - |
Cereibacter sphaeroides | ubiquinone + 2 ferrocyanide + 2 H+ | - |
? | |
| 7.1.1.8 | ubiquinol + 2 ferricytochrome c | - |
Bos taurus | ubiquinone + 2 ferrocytochrome c + 2 H+ | - |
? | |
| 7.1.1.8 | ubiquinol + 2 ferricytochrome c | - |
Cereibacter sphaeroides | ubiquinone + 2 ferrocytochrome c + 2 H+ | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 7.1.1.8 | More | the Rhodobacter sphaeroides complex contains four protein subunits: three core subunits and one supernumerary subunit | Cereibacter sphaeroides |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 7.1.1.8 | bc1 | - |
Bos taurus |
| 7.1.1.8 | bc1 | - |
Cereibacter sphaeroides |
| 7.1.1.8 | cytochrome bc1 complex | - |
Bos taurus |
| 7.1.1.8 | cytochrome bc1 complex | - |
Cereibacter sphaeroides |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 7.1.1.8 | 23 | - |
assay at | Bos taurus |
| 7.1.1.8 | 23 | - |
assay at | Cereibacter sphaeroides |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 7.1.1.8 | 7.4 | - |
assay at | Bos taurus |
| 7.1.1.8 | 7.4 | - |
assay at | Cereibacter sphaeroides |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 7.1.1.8 | malfunction | when the only supernumerary subunit (subunit IV) is deleted from the Rhodobaacter sphaeroides wild-type complex, the resulting three-subunit core complex has only a fraction of the electron transfer activity of the wild-type complex but has about four times the superoxide anions generating activity. When the three-subunit core complex is reconstituted with subunit IV, the electron transfer activity increases, and the O2 -.-generating activity decreases to the same level as those in the wild-type, four-subunit complex | Cereibacter sphaeroides |
| 7.1.1.8 | physiological function | reaction mechanism of superoxide generation by bc1, overview | Cereibacter sphaeroides |
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