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Literature summary for 7.1.1.9 extracted from

  • Sedlak, E.; Varhac, R.; Musatov, A.; Robinson, N.C.
    The kinetic stability of cytochrome C oxidase effect of bound phospholipid and dimerization (2014), Biophys. J., 107, 2941-2949 .
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial membrane
-
Bos taurus 31966
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ferrocytochrome c + O2 + H+ Bos taurus
-
ferricytochrome c + H2O
-
?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
HiTrap Q column chromatography Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ferrocytochrome c + O2 + H+
-
Bos taurus ferricytochrome c + H2O
-
?

Synonyms

Synonyms Comment Organism
CCO
-
Bos taurus
cytochrome c oxidase
-
Bos taurus
ferrocytochrome c: O2 oxidoreductase
-
Bos taurus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
37 61 the half-life of the enzyme at 37°C is 0.4 h, the dissociation of subunit III and/or VIIa is responsible for temperature-induced inactivation of the enzyme at 61°C Bos taurus