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Literature summary extracted from

  • Jasaitis, A.; Backgren, C.; Morgan, J.E.; Puustinen, A.; Verkhovsky, M.I.; Wikstroem, M.
    Electron and Proton Transfer in the Arginine-54-Methionine Mutant of Cytochrome c Oxidase from Paracoccus denitrificans (2001), Biochemistry, 40, 5269-5274.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
7.1.1.9 R54M low turnover number, changes in spectral properties of heme a, lowered midpoint redox potential, electron transfer from CuA to heme a is impaired Paracoccus denitrificans

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.9 Paracoccus denitrificans
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.1.9 ferrocytochrome c + O2 + H+
-
Paracoccus denitrificans 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 20
-
ferrocytochrome c R54M mutant enzyme Paracoccus denitrificans