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Literature summary extracted from

  • Mogi, T.; Sato-Watanabe, M.; Miyoshi, H.; Orii, Y.
    Role of a bound ubiquinone on reactions of the Escherichia coli cytochrome bo with ubiquinol and dioxygen (1999), FEBS Lett., 457, 223-226.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.3 Escherichia coli
-
-
-
7.1.1.3 Escherichia coli GO103/pHN3795-1
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.1.1.3
-
 Escherichia coli

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 GO103/pHN3795-1 ubiquinone-1 + H2O + H+/out
-
 ?

Synonyms

EC Number Synonyms Comment Organism
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 in subunit I Escherichia coli
7.1.1.3 ubiquinone-8 the bound ubiquinone at the QH site of cytochrome bo is essential for the catalytic turnover of the oxidase reactions, but it is not necessary for re-reduction of ferric heme b after the heme b-to-heme o electron transfer under flow-flash conditions Escherichia coli