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Literature summary 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

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

Localization

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

Metals/Ions

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

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.3 Escherichia coli
-
-
-
7.1.1.3 Escherichia coli ST4676
-
-
-

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
7.1.1.3 bo-type ubiquinol oxidase
-
 Escherichia coli
7.1.1.3 cytochrome bo
-
 Escherichia coli

Cofactor

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

General Information

EC Number General Information Comment Organism
7.1.1.3 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