Literature summary for 7.1.1.3 extracted from

Calhoun, M.W.; Hill, J.J.; Lemieux, L.J.; Ingledew, W.J.; Alben, J.O.; Gennis, R.B.
Site-directed mutants of the cytochrome bo ubiquinol oxidase of Escherichia coli: amino acid substitutions for two histidines that are putative CuB ligands (1993), Biochemistry, 32, 11524-11529.

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Protein Variants

Protein Variants	Comment	Organism
H333C	nonfunctional enzyme	Escherichia coli
H333L	the mutation eliminates the magnetic coupling between heme o and CuB leading to a nonfunctional enzyme	Escherichia coli
H333N	nonfunctional enzyme	Escherichia coli
H333Q	nonfunctional enzyme	Escherichia coli
H334L	the mutation eliminates the magnetic coupling between heme o and CuB leading to a nonfunctional enzyme	Escherichia coli
H334M	nonfunctional enzyme	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
copper	the high-spin heme is magnetically coupled to a copper, CuB, forming a binuclear center which is the site of oxygen reduction to water	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-
Escherichia coli GLlOl	-	-	-

Synonyms

Synonyms	Comment	Organism
cytochrome bo ubiquinol oxidase	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
heme	the high-spin heme is magnetically coupled to a copper, CuB, forming a binuclear center which is the site of oxygen reduction to water	Escherichia coli

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Release 2023.1 (January 2023)