Literature summary for 7.1.1.9 extracted from

De Vrij, W.; Konings, W.N.
Kinetic characterization of cytochrome c oxidase from Bacillus subtilis (1987), Eur. J. Biochem., 166, 581-587.

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KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0045	-	ferrocytochrome c	yeast cytochrome c	Bacillus subtilis
0.0055	-	ferrocytochrome c	horse heart cytochrome c	Bacillus subtilis
0.015	-	ferrocytochrome c	yeast cytochrome c, in the presence of 100 mM KCl	Bacillus subtilis
0.016	-	ferrocytochrome c	horse heart cytochrome c, in the presence of 50 mM KCl	Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
290000	315000	gel filtration, value depending on ionic strength	Bacillus subtilis

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	-	-	-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
2.08	2.58	ferrocytochrome c	-	Bacillus subtilis
13.3	16	ferrocytochrome c	enzyme reconstituted into asolectin liposomes	Bacillus subtilis

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Release 2023.1 (January 2023)