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Literature summary extracted from

  • De Vrij, W.; Konings, W.N.
    Kinetic characterization of cytochrome c oxidase from Bacillus subtilis (1987), Eur. J. Biochem., 166, 581-587.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.1.1.9 0.0045
-
ferrocytochrome c yeast cytochrome c Bacillus subtilis
7.1.1.9 0.0055
-
ferrocytochrome c horse heart cytochrome c Bacillus subtilis
7.1.1.9 0.015
-
ferrocytochrome c yeast cytochrome c, in the presence of 100 mM KCl Bacillus subtilis
7.1.1.9 0.016
-
ferrocytochrome c horse heart cytochrome c, in the presence of 50 mM KCl Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
7.1.1.9 290000 315000 gel filtration, value depending on ionic strength Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.9 Bacillus subtilis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.1.9 ferrocytochrome c + O2 + H+
-
Bacillus subtilis ferricytochrome c + H2O
-
r

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
7.1.1.9 2.08 2.58 ferrocytochrome c
-
Bacillus subtilis
7.1.1.9 13.3 16 ferrocytochrome c enzyme reconstituted into asolectin liposomes Bacillus subtilis