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Literature summary for 7.1.1.3 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
Search for more literature for 7.1.1.3

Crystallization (Commentary)

Crystallization (Comment) Organism
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

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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
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
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
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
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

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Escherichia coli P0ABJ1
-
-

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
-
 ?

Subunits

Subunits Comment Organism
tetramer x-ray crystallography Escherichia coli

Synonyms

Synonyms Comment Organism
cytochrome bo3
-
 Escherichia coli
ubiquinol oxidase
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
heme heme b and heme o3 Escherichia coli

General Information

General Information Comment Organism
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