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Literature summary for 7.1.1.3 extracted from

  • Kawasaki, M.; Mogi, T.; Anraku, Y.
    Substitutions of charged amino acid residues conserved in subunit I perturb the redox metal centers of the Escherichia coli bo-type ubiquinol oxidase (1997), J. Biochem., 122, 422-429.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D135N the mutations specifically eliminates the CuB center from the oxidase complex Escherichia coli
D188N the mutant possesses 100% copper and 81% cytochrome o compared to the wild type enzyme Escherichia coli
D256N the mutant possesses 103% copper and 74% cytochrome o compared to the wild type enzyme Escherichia coli
D407N the mutation affects the CO-binding by the heme-copper binuclear center Escherichia coli
E286D the mutant does not show significant perturbations on the redox metal centers even though it is still inactive Escherichia coli
E286Q the mutations specifically eliminates the CuB center from the oxidase complex Escherichia coli
E540Q the mutation affects the CO-binding by the heme-copper binuclear center Escherichia coli
K362Q the mutation affects the CO-binding by the heme-copper binuclear center Escherichia coli
K55Q the mutant possesses 100% copper and 73% cytochrome o compared to the wild type enzyme Escherichia coli
R257Q the mutations specifically eliminates the CuB center from the oxidase complex Escherichia coli
R481Q the mutant possesses 91% copper and 73% cytochrome o compared to the wild type enzyme Escherichia coli
R482Q the mutant possesses 82% copper and 100% cytochrome o compared to the wild type enzyme Escherichia coli
R80Q the mutation causes loss of a diagnostic peak for low-spin heme b in the 77 K redox difference spectrum Escherichia coli
Y173F the mutant possesses 91% copper and 108% cytochrome o compared to the wild type enzyme Escherichia coli
Y288F the mutations specifically eliminates the CuB center from the oxidase complex Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasmic membrane
-
Escherichia coli
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
copper the enzyme contains CuB Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli ST4676
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ubiquinol-1 + O2 + H+/in
-
Escherichia coli ubiquinone-1 + H2O + H+/out
-
?
ubiquinol-1 + O2 + H+/in
-
Escherichia coli ST4676 ubiquinone-1 + H2O + H+/out
-
?

Synonyms

Synonyms Comment Organism
bo-type ubiquinol oxidase
-
Escherichia coli
cytochrome bo
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
heme low-spin heme b and high-spin heme o Escherichia coli

General Information

General Information Comment Organism
physiological function cytochrome bo is a four-subunit quinol oxidase in the aerobic respiratory chain of Escherichia coli and functions as a redox-coupled proton pump Escherichia coli