Literature summary for 7.1.1.9 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.

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Protein Variants

Protein Variants	Comment	Organism
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

Organism	UniProt	Comment	Textmining
Paracoccus denitrificans	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ferrocytochrome c + O2 + H+	-	Paracoccus denitrificans	ferricytochrome c + H2O	-	r

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
20	-	ferrocytochrome c	R54M mutant enzyme	Paracoccus denitrificans

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Release 2023.1 (January 2023)