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Literature summary extracted from

  • Zhou, F.; Yin, Y.; Su, T.; Yu, L.; Yu, C.A.
    Oxygen dependent electron transfer in the cytochrome bc complex (2012), Biochim. Biophys. Acta, 1817, 2103-2109.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
7.1.1.8 O2 molecular oxygen increases the activity of Rhodobacter sphaeroides bc1 complex up to 82%, depending on the intactness of the complex. Since oxygen enhances the reduction rate of heme bL, but shows no effect on the reduction rate of heme bH, the effect of oxygen in the electron transfer sequence of the cytochrome bc1 complex is at the step of heme bL reduction during bifurcated oxidation of ubiquinol. Free superoxide anion is not involved in the oxygen enhanced reduction of heme bL Cereibacter sphaeroides

Protein Variants

EC Number Protein Variants Comment Organism
7.1.1.8 H111N site-directed mutagenesis, the rate of heme bL reduction in the H111N mutant complex increases in the presence of oxygen, no altered effect of superoxide dismutase on the oxygen increased rate of heme bL reduction in the H111N mutant complex compaired to the wild-type enzyme, overview 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 pre-steady state reduction rate of cytochrome bL in bc1 complex by ubiquinol and effect of oxygen on the kinetics, overview Cereibacter sphaeroides

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.1.1.8 Fe2+ Rieske iron-sulfur protein possessing a high potential [2Fe-2S] cluster Cereibacter sphaeroides

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 Cereibacter sphaeroides
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 all the bc1 complexes contain three redox prosthetic group bearing subunits (cytochrome b, cytochrome c1, and Rieske iron-sulfur protein) with varying numbers (ranging from 0 to 8) of non-redox prosthetic group bearing (supernumerary) subunits Cereibacter sphaeroides

Cofactor

EC Number Cofactor Comment Organism Structure
7.1.1.8 cytochrome b the cytochrome b subunit contains two b-type hemes, bL and bH Cereibacter sphaeroides
7.1.1.8 cytochrome c1 the cytochrome c1 subunit carries a c-type heme (c1) Cereibacter sphaeroides
7.1.1.8 additional information all the bc1 complexes contain three redox prosthetic group bearing subunits (cytochrome b, cytochrome c1, and Rieske iron-sulfur protein) with varying numbers (ranging from 0 to 8) of non-redox prosthetic group bearing (supernumerary) subunits Cereibacter sphaeroides

General Information

EC Number General Information Comment Organism
7.1.1.8 physiological function the cytochrome bc1 complex is an essential energy transduction electron transfer complex in photosynthetic bacteria. This complex catalyzes the electron transfer from ubiquinol to cytochrome c (or c2) with concomitant generation of a proton gradient and membrane potential for ATP synthesis by the ATP synthase complex Cereibacter sphaeroides