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Literature summary extracted from

  • Crofts, A.R.
    Proton-coupled electron transfer at the Qo-site of the bc1 complex controls the rate of ubihydroquinone oxidation (2004), Biochim. Biophys. Acta, 1655, 77-92.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
7.1.1.8 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
7.1.1.8 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
7.1.1.8 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
7.1.1.8 Y156W site-directed mutagenesis, mutant enzyme shows altered pH-dependence compared to the wild-type enzyme Cereibacter sphaeroides

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.1.1.8 5-undecyl-6-hydroxy-4,7-dioxobenzothiazol
-
Cereibacter sphaeroides
7.1.1.8 additional information inhibitor binding at the quinone reduction Qi side or the quinol oxidation Qo side Cereibacter sphaeroides
7.1.1.8 Myxothiazol
-
Cereibacter sphaeroides
7.1.1.8 Stigmatellin binding involves conformational change of Glu295, molecular dynamic simulation, mutants E295G, E295D, and E295Q are resistant to inhibition Cereibacter sphaeroides

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.1.1.8 additional information
-
additional information reaction kinetics of oxidation and electron transfer, complex formation kinetics, pH-dependence Cereibacter sphaeroides

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.1.1.8 mitochondrion
-
Cereibacter sphaeroides 5739
-

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 the Qo-cycle, overview ?
-
?
7.1.1.8 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

EC Number Organism UniProt Comment Textmining
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] 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 and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.1.8 additional information the Qo-cycle, overview Cereibacter sphaeroides ?
-
?
7.1.1.8 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+
-
?
7.1.1.8 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

EC Number Synonyms Comment Organism
7.1.1.8 bc1 complex
-
Cereibacter sphaeroides
7.1.1.8 cytochrome bc1 complex
-
Cereibacter sphaeroides

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
7.1.1.8 additional information
-
additional information inhibitor binding and inhibition kinetics Cereibacter sphaeroides