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Literature summary for 7.1.1.3 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
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Protein Variants

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli GO103/pMFO2
-
-
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
tetramer
-
 Escherichia coli

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