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Literature summary extracted from

  • Abramson, J.; Riistama, S.; Larsson, G.; Jasaitis, A.; Svensson-Ek, M.; Laakkonen, L.; Puustinen, A.; Iwata, S.; Wikstrom, M.
    The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site (2000), Nat. Struct. Biol., 7, 910-917.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
7.1.1.3 hanging drop vapor diffusion method, using 9-10% (w/v) PEG 1500, 100 mM NaCl, 100 mM MgCl2 and 5% (v/v) ethanol Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
7.1.1.3 D75N the mutation inhibits activity by 99% Escherichia coli
7.1.1.3 H98N the mutation inhibits activity by 97% Escherichia coli
7.1.1.3 Q101N the mutation inhibits activity by 75% and causes a 10fold increase in the apparent KM for ubiquinol-1 Escherichia coli
7.1.1.3 R71L the mutation inhibits activity by 99% Escherichia coli
7.1.1.3 R71Q the mutation inhibits activity by 99% Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.1.1.3 0.018
-
 ubiquinol-1 wild type enzyme, when Triton X-100 is used as detergent in the isolation of the enzyme, in 50 mM Tris-HCl, pH 7.4, at 25°C Escherichia coli
7.1.1.3 0.023
-
 ubiquinol-1 mutant enzyme Q101N, when Triton X-100 is used as detergent in the isolation of the enzyme, in 50 mM Tris-HCl, pH 7.4, at 25°C Escherichia coli
7.1.1.3 0.024
-
 ubiquinol-1 mutant enzyme Q101N, when 0.02% (v/v) n-dodecyl beta-D-maltoside is used as detergent in the isolation of the enzyme, in 50 mM Tris-HCl, pH 7.4, at 25°C Escherichia coli
7.1.1.3 0.045
-
 ubiquinol-1 wild type enzyme, when 0.02% (v/v) n-dodecyl beta-D-maltoside is used as detergent in the isolation of the enzyme, in 50 mM Tris-HCl, pH 7.4, at 25°C Escherichia coli
7.1.1.3 0.175
-
 ubiquinol-1 mutant enzyme H98N, when 0.02% (v/v) n-dodecyl beta-D-maltoside is used as detergent in the isolation of the enzyme, in 50 mM Tris-HCl, pH 7.4, at 25°C Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.1.1.3 membrane
-
 Escherichia coli 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.1.1.3 copper the enzyme is a four-subunit heme-copper oxidase containing CuB Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.3 Escherichia coli P0ABJ1
-
-

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
-
 ?

Subunits

EC Number Subunits Comment Organism
7.1.1.3 tetramer x-ray crystallography Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
7.1.1.3 cytochrome bo3
-
 Escherichia coli
7.1.1.3 ubiquinol oxidase
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
7.1.1.3 heme heme b and heme o3 Escherichia coli

General Information

EC Number General Information Comment Organism
7.1.1.3 physiological function cytochrome bo3 ubiquinol oxidase from Escherichia coli is a four-subunit heme-copper oxidase that catalyzes the four-electron reduction of O2 to water and functions as a proton pump Escherichia coli