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Literature summary extracted from

  • Mogi, T.; Minagawa, J.; Hirano, T.; Sato-Watanabe, M.; Tsubaki, M.; Uno, T.; Hori, H.; Nakamura, H.; Nishimura, Y.; Anraku, Y.
    Substitutions of conserved aromatic amino acid residues in subunit I perturb the metal centers of the Escherichia coli bo-type ubiquinol oxidase (1998), Biochemistry, 37, 1632-1639.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
7.1.1.3 F112L the mutation does not affect the in vivo activity Escherichia coli
7.1.1.3 F113L the mutation does not affect the in vivo activity Escherichia coli
7.1.1.3 F208L the mutation does not affect the in vivo activity Escherichia coli
7.1.1.3 F295L the mutation does not affect the in vivo activity Escherichia coli
7.1.1.3 F336L the mutation does not affect the in vivo activity Escherichia coli
7.1.1.3 F347L the mutation does not affect the in vivo activity Escherichia coli
7.1.1.3 F348L 4.8% activity compared to the wild type enzyme Escherichia coli
7.1.1.3 F391L the mutation does not affect the in vivo activity Escherichia coli
7.1.1.3 F415W the mutation does not affect the in vivo activity Escherichia coli
7.1.1.3 F420L the mutation does not affect the in vivo activity Escherichia coli
7.1.1.3 W147L the mutation does not affect the in vivo activity Escherichia coli
7.1.1.3 W280L 67% activity compared to the wild type enzyme Escherichia coli
7.1.1.3 W282F the mutation does not affect the in vivo activity Escherichia coli
7.1.1.3 W331L 19% activity compared to the wild type enzyme Escherichia coli
7.1.1.3 Y288L 0.3% activity compared to the wild type enzyme Escherichia coli
7.1.1.3 Y61F the mutation does not affect the in vivo activity Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.1.1.3 Cu2+ the enzyme contains 6.78 nmol copper per mg of protein Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.3 Escherichia coli
-
-
-
7.1.1.3 Escherichia coli GO103/pMFO2
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.1.3 ubiquinol + O2 + H+/in
-
 Escherichia coli ubiquinone + H2O + H+/out
-
 ?
7.1.1.3 ubiquinol + O2 + H+/in
-
 Escherichia coli GO103/pMFO2 ubiquinone + H2O + H+/out
-
 ?

Subunits

EC Number Subunits Comment Organism
7.1.1.3 tetramer
-
 Escherichia coli

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