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Literature summary for 7.1.1.8 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
Search for more literature for 7.1.1.8

Activating Compound

Activating Compound Comment Organism Structure
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

Protein Variants Comment Organism
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ubiquinol + 2 ferricytochrome c Cereibacter sphaeroides
-
 ubiquinone + 2 ferrocytochrome c + 2 H+
-
 ?

Organism

Organism UniProt Comment Textmining
Cereibacter sphaeroides
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ubiquinol + 2 ferricytochrome c
-
 Cereibacter sphaeroides ubiquinone + 2 ferrocytochrome c + 2 H+
-
 ?

Subunits

Subunits Comment Organism
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

Cofactor Comment Organism Structure
cytochrome b the cytochrome b subunit contains two b-type hemes, bL and bH Cereibacter sphaeroides
cytochrome c1 the cytochrome c1 subunit carries a c-type heme (c1) Cereibacter sphaeroides
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

General Information Comment Organism
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