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Literature summary for 7.1.1.3 extracted from

  • Siletsky, S.A.; Dyuba, A.V.; Elkina, D.A.; Monakhova, M.V.; Borisov, V.B.
    Spectral-kinetic analysis of recombination reaction of heme centers of bd-type quinol oxidase from Escherichia coli with carbon monoxide (2017), Biochemistry, 82, 1354-1366 .
    View publication on PubMed
Search for more literature for 7.1.1.3

Protein Variants

Protein Variants Comment Organism
D75H mutant exhibits broad i-V curves with half-wave potentials shifted toward more positive potentials Escherichia coli
F93Y mutant exhibits good electrocatalytic performance and a well-defined sigmoidal i-V curve. Compared to wild-type, the half-wave potential is downshifted by up to 40 mV Escherichia coli
H98F mutant exhibits broad i-V curves with half-wave potentials shifted toward more positive potentials Escherichia coli
I102W mutant exhibits broad i-V curves with half-wave potentials shifted toward more positive potentials Escherichia coli
Q101A mutant exhibits good electrocatalytic performance and a well-defined sigmoidal i-V curve. Compared to wild-type, the half-wave potential is downshifted by up to 40 mV Escherichia coli
Q101L mutant exhibits good electrocatalytic performance and a well-defined sigmoidal i-V curve. Compared to wild-type, the half-wave potential is downshifted by up to 40 mV Escherichia coli
R71H mutant exhibits broad i-V curves with half-wave potentials shifted toward more positive potentials Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0ABI8
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ubiquinol + n H+ + O2
-
 Escherichia coli 2 ubiquinone + n H+ + 2 H2O
-
 ?

Synonyms

Synonyms Comment Organism
cyoB
-
 Escherichia coli
cytochrome bo(3) ubiquinol oxidase
-
 Escherichia coli

General Information

General Information Comment Organism
physiological function in the absence of the tightly bound quinone, a strongly diminished rate of electrocatalytic reduction of oxygen is detected, which can be restored by adding quinones. The stabilization of the radical is not necessary for the oxygen reaction. The reaction mechanism should involve a one electron transfer step from the quinone radical to the next electron acceptor, the heme b Escherichia coli