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Literature summary extracted from

  • Höchli, L.; Hackenbrock, C.R.
    Cytochrome c oxidase from rat liver mitochondria: purification and characterization (1978), Biochemistry, 17, 3712-3719.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
7.1.1.9 asolectin 20-30% more activity in the presence of asolectin Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.1.1.9 0.01 0.015 ferrocytochrome c
-
 Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.9 Rattus norvegicus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
7.1.1.9 phospholipoprotein 0.037 mg/mg enzyme Rattus norvegicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
7.1.1.9 liver
-
 Rattus norvegicus
-

Storage Stability

EC Number Storage Stability Organism
7.1.1.9 0°C, 100 mM, potassium phosphate, pH 7.4, 0.5% Tween 20, 6 d, 40-50% loss of activity Rattus norvegicus

Substrates and Products (Substrate)

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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
7.1.1.9 133
-
 ferrocytochrome c
-
 Rattus norvegicus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
7.1.1.9 6 6.3
-
 Rattus norvegicus