Literature summary for 7.1.1.3 extracted from

Egawa, T.; Lin, M.T.; Hosler, J.P.; Gennis, R.B.; Yeh, S.R.; Rousseau, D.L.
Communication between R481 and CuB in cytochrome bo3 ubiquinol oxidase from Escherichia coli (2009), Biochemistry, 48, 12113-12124.

Search for more literature for 7.1.1.3

Protein Variants

Protein Variants	Comment	Organism
R481L	nonfunctional mutant	Escherichia coli
R481Q	the mutant is fully functional	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
copper	the enzyme has a CuB site	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Synonyms

Synonyms	Comment	Organism
cytochrome bo3 ubiquinol oxidase	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
heme	heme b and heme o3	Escherichia coli

General Information

General Information	Comment	Organism
physiological function	cytochrome bo3 ubiquinol oxidase serves as part of a proton loading site that regulates proton translocation across the protein matrix of the enzyme	Escherichia coli

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Release 2023.1 (January 2023)