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Literature summary for 7.1.1.3 extracted from

  • Belevich, I.; Borisov, V.B.; Zhang, J.; Yang, K.; Konstantinov, A.A.; Gennis, R.B.; Verkhovsky, M.I.
    Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site (2005), Proc. Natl. Acad. Sci. USA, 102, 3657-3662.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
E445A heme b595 is present in the E445A mutant. Formation of the oxoferryl state in the mutant is about 100fold slower than in the wild type enzyme. The E445A substitution does not affect intraprotein electron re-equilibration after the photolysis of CO bound to ferrous heme d in the one-electron-reduced enzyme. The mutation does not affect membrane potential generation coupled to intramolecular electron redistribution between hemes d2+ and b558 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli GO105
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information electron transfer between hemes d and b595 is not electrogenic, although heme b595 is the major electron acceptor for heme d during the backflow, and therefore is not likely to be accompanied by net H+ uptake or release Escherichia coli ?
-
 ?
additional information electron transfer between hemes d and b595 is not electrogenic, although heme b595 is the major electron acceptor for heme d during the backflow, and therefore is not likely to be accompanied by net H+ uptake or release Escherichia coli GO105 ?
-
 ?

Synonyms

Synonyms Comment Organism
bd-type quinol oxidase
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
heme heme d and heme b558 Escherichia coli