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Literature summary for 7.1.1.9 extracted from

  • Hilbers, F.; Von Der Hocht, I.; Ludwig, B.; Michel, H.
    True wild type and recombinant wild type cytochrome c oxidase from Paracoccus denitrificans show a 20-fold difference in their catalase activity (2013), Biochim. Biophys. Acta, 1827, 319-327 .
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli DH5alpha cells Paracoccus denitrificans

Metals/Ions

Metals/Ions Comment Organism Structure
Cu contains copper Paracoccus denitrificans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ferrocytochrome c + O2 + H+ Paracoccus denitrificans
-
ferricytochrome c + H2O
-
?
additional information Paracoccus denitrificans the enzyme also shows catalase activity ?
-
?

Organism

Organism UniProt Comment Textmining
Paracoccus denitrificans
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Strep-Tactin column chromatography Paracoccus denitrificans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ferrocytochrome c + O2 + H+
-
Paracoccus denitrificans ferricytochrome c + H2O
-
?
additional information the enzyme also shows catalase activity Paracoccus denitrificans ?
-
?

Synonyms

Synonyms Comment Organism
CCO
-
Paracoccus denitrificans
cytochrome c oxidase
-
Paracoccus denitrificans

Cofactor

Cofactor Comment Organism Structure
heme
-
Paracoccus denitrificans