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Literature summary for 7.1.1.3 extracted from

  • Tsubaki, M.; Hori, H.; Mogi, T.
    Glutamate-286 mutants of cytochrome bo-type ubiquinol oxidase from Escherichia coli: influence of mutations on the binuclear center structure revealed by FT-IR and EPR spectroscopies (1997), FEBS Lett., 416, 247-250.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
E286A inactive Escherichia coli
E286D the mutant retains 31% of the wild type activity Escherichia coli
E286Q the mutant shows 4% activity compared to the wild type enzyme and is unable to bind azide ions Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
cyanide
-
Escherichia coli

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
copper the enzyme is a heme-copper terminal oxidase Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli GO103
-
-
-

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 GO103 ubiquinone-1 + H2O + H+/out
-
?
ubiquinol-8 + O2 + H+/in
-
Escherichia coli ubiquinone-8 + H2O + H+/out
-
?
ubiquinol-8 + O2 + H+/in
-
Escherichia coli GO103 ubiquinone-8 + H2O + H+/out
-
?

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
heme hemes B and O Escherichia coli
ubiquinol-8
-
Escherichia coli

General Information

General Information Comment Organism
physiological function cytochrome bo-type ubiquinol oxidase in the aerobic respiratory chain of Escherichia coli catalyzes the reduction of dioxygen to water with ubiquinol-8, and utilizes the redox reactions to drive vectorial translocation of protons across the cytoplasmic membrane Escherichia coli