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Literature summary for 7.1.1.8 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
Search for more literature for 7.1.1.8

Protein Variants

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

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 [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

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

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Cereibacter sphaeroides
-
-
-

Reaction

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
a

Substrates and Products (Substrate)

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

Synonyms Comment Organism
bc1 complex
-
 Cereibacter sphaeroides
cytochrome bc1 complex
-
 Cereibacter sphaeroides

Ki Value [mM]

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