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Literature summary for 7.1.1.3 extracted from

  • Garcia-Horsman, J.; Puustinen, A.; Gennis, R.; Wikstrom, M.
    Proton transfer in cytochrome bo3 ubiquinol oxidase of Escherichia coli: second-site mutations in subunit I that restore proton pumping in the mutant Asp135-->Asn (1995), Biochemistry, 34, 4428-4433.
    View publication on PubMed
Search for more literature for 7.1.1.3

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli RG 129 cells Escherichia coli

Protein Variants

Protein Variants Comment Organism
D135K the mutant is deficient in proton pumping (23% activity compared to the wild type enzyme) Escherichia coli
D135N the mutant is deficient in proton pumping (45% activity compared to the wild type enzyme) Escherichia coli
F138G the mutant shows 63% proton-translocating activity compared to the wild type enzyme Escherichia coli
F138R the mutant shows 55% proton-translocating activity compared to the wild type enzyme Escherichia coli
G132A the mutant shows wild type proton-translocation activity (113% activity compared to the wild type enzyme) Escherichia coli
G132D/D135N the mutant shows 66% proton-translocating activity compared to the wild type enzyme Escherichia coli
G132R the mutant shows wild type proton-translocation activity Escherichia coli
K362D/Dl35K the mutant is devoid of redox activity Escherichia coli
N124D the mutant is deficient in proton pumping (56% activity compared to the wild type enzyme) Escherichia coli
N124D/D135N the mutant shows 21% proton-translocating activity compared to the wild type enzyme Escherichia coli
N124H the mutant is deficient in proton pumping (16% activity compared to the wild type enzyme) Escherichia coli
N142D the mutant is deficient in proton pumping (48% activity compared to the wild type enzyme) Escherichia coli
N142D/D135N the mutant shows 33% proton-translocating activity compared to the wild type enzyme Escherichia coli
N142Q the mutant shows wild type proton-translocation activity (109% activity compared to the wild type enzyme) Escherichia coli
N142V the mutant is deficient in proton pumping (22% activity compared to the wild type enzyme) Escherichia coli
P128A the mutant shows wild type proton-translocation activity (115% activity compared to the wild type enzyme) Escherichia coli
P128D/D135N inactive Escherichia coli
P139E/D135N the mutant shows 95% proton-translocating activity compared to the wild type enzyme Escherichia coli
Pl39A the mutant shows wild type proton-translocation activity (67% activity compared to the wild type enzyme) Escherichia coli
Pl39E the mutant shows wild type proton-translocation activity (46% activity compared to the wild type enzyme) Escherichia coli
R134P the mutant shows 112% proton-translocating activity compared to the wild type enzyme Escherichia coli

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ the ubiquinol oxidase cytochrome b03 of Escherichia coli is a member of the respiratory heme-copper oxidase family Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
cytochrome bo3 ubiquinol oxidase
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
heme the ubiquinol oxidase cytochrome b03 of Escherichia coli is a member of the respiratory heme-copper oxidase family Escherichia coli

General Information

General Information Comment Organism
physiological function the ubiquinol oxidase, cytochrome b03, of Escherichia coli is a member of the respiratory heme-copper oxidase family and conserves energy from the reduction of dioxygen to water by translocation of protons across the bacterial membrane Escherichia coli