Protein Variants | Comment | Organism |
---|---|---|
E295D | site-directed mutagenesis, mutant is insensitive to stigmatellin inhibition, mutant shows slightly increased Km for ubiquinol, and lowered electron transfer rates compared to the wild-type | Cereibacter sphaeroides |
E295G | site-directed mutagenesis, mutant is insensitive to stigmatellin inhibition, mutant shows slightly increased Km for ubiquinol, and lowered electron transfer rates compared to the wild-type | Cereibacter sphaeroides |
E295Q | site-directed mutagenesis, mutant is insensitive to stigmatellin inhibition, mutant shows slightly increased Km for ubiquinol, and lowered electron transfer rates compared to the wild-type | Cereibacter sphaeroides |
Y156W | site-directed mutagenesis, mutant enzyme shows altered pH-dependence compared to the wild-type enzyme | Cereibacter sphaeroides |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
5-undecyl-6-hydroxy-4,7-dioxobenzothiazol | - |
Cereibacter sphaeroides | |
additional information | inhibitor binding at the quinone reduction Qi side or the quinol oxidation Qo side | Cereibacter sphaeroides | |
Myxothiazol | - |
Cereibacter sphaeroides | |
Stigmatellin | binding involves conformational change of Glu295, molecular dynamic simulation, mutants E295G, E295D, and E295Q are resistant to inhibition | Cereibacter sphaeroides |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | reaction kinetics of oxidation and electron transfer, complex formation kinetics, pH-dependence | Cereibacter sphaeroides |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | - |
Cereibacter sphaeroides | 5739 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Cereibacter sphaeroides | the Qo-cycle, overview | ? | - |
? | |
ubiquinol-2 + 2 ferricytochrome c | Cereibacter sphaeroides | proton-coupled electron transfer at the Qo-site of the bc1 complex controls the rate of ubihydroquinone oxidation | ubiquinone-2 + 2 ferrocytochrome c + 2 H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Cereibacter sphaeroides | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+[side 2] | the Qo-cycle, overview, reaction mechanism involving cytochrome c, Glu295, and His161, electron transfer mechanism and formation of the ES complex involving a binding square, substrate binding mechanism at the Qo site of the cytochrome bc1 complex | Cereibacter sphaeroides |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the Qo-cycle, overview | Cereibacter sphaeroides | ? | - |
? | |
ubiquinol-2 + 2 ferricytochrome c | proton-coupled electron transfer at the Qo-site of the bc1 complex controls the rate of ubihydroquinone oxidation | Cereibacter sphaeroides | ubiquinone-2 + 2 ferrocytochrome c + 2 H+ | - |
? | |
ubiquinol-2 + 2 ferricytochrome c | rate-limiting is the transfer of the first electron from ubiquinol to the [2Fe-2S] cluster of the Rieske iron-sulfur-protein at the Qo-side, reaction energy profile | Cereibacter sphaeroides | ubiquinone-2 + 2 ferrocytochrome c + 2 H+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
bc1 complex | - |
Cereibacter sphaeroides |
cytochrome bc1 complex | - |
Cereibacter sphaeroides |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | inhibitor binding and inhibition kinetics | Cereibacter sphaeroides |