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Literature summary 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

Protein Variants

EC Number Protein Variants Comment Organism
7.1.1.3 D75H mutant exhibits broad i-V curves with half-wave potentials shifted toward more positive potentials Escherichia coli
7.1.1.3 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
7.1.1.3 H98F mutant exhibits broad i-V curves with half-wave potentials shifted toward more positive potentials Escherichia coli
7.1.1.3 I102W mutant exhibits broad i-V curves with half-wave potentials shifted toward more positive potentials Escherichia coli
7.1.1.3 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
7.1.1.3 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
7.1.1.3 R71H mutant exhibits broad i-V curves with half-wave potentials shifted toward more positive potentials Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.3 Escherichia coli P0ABI8
-
-
7.1.1.7 Escherichia coli P0ABJ9 and P0ABK2 and P56100 P0ABJ9 i.e. subunit cydA, P0ABK2 i.e. subunit cydB, P56100 i.e. subunit cydX
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.1.1.3
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.1.3 2 ubiquinol + n H+ + O2
-
 Escherichia coli 2 ubiquinone + n H+ + 2 H2O
-
 ?

Synonyms

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

General Information

EC Number General Information Comment Organism
7.1.1.3 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
7.1.1.7 physiological function the unresolved photodissociation of CO is followed by a four-phased recombination with characteristic times of about 20 micros, 250 micros, 1.1 ms, and 24 ms. The 20x02micros phase most likely reflects bimolecular recombination of CO with heme d. The 250x02micros phase is heterogeneous and includes recombination of CO with about 7% of heme b595 and transition of heme d from a pentacoordinate to a transient hexacoordinate state in this enzyme population. The 24x02ms transition probably reflects a return of heme d to the pentacoordinate state in the same protein fraction. The 1.1x02ms phase reflects a recombination of CO with about 15% of heme b558 Escherichia coli