Thermodynamics of electron transfer in Escherichia coli cytochrome bo3
AUTOR(ES)
Schultz, Brian E.
FONTE
The National Academy of Sciences
RESUMO
The proton translocation mechanism of the Escherichia coli cytochrome bo3 complex is intimately tied to the electron transfers within the enzyme. Herein we evaluate two models of proton translocation in this enzyme, a cytochrome c oxidase-type ion-pump and a Q-cycle mechanism, on the basis of the thermodynamics of electron transfer. We conclude that from a thermodynamic standpoint, a Q-cycle is the more favorable mechanism for proton translocation and is likely occurring in the enzyme.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=21694Documentos Relacionados
- Reaction of the Escherichia coli quinol oxidase cytochrome bo3 with dioxygen: the role of a bound ubiquinone molecule.
- Glutamic acid 286 in subunit I of cytochrome bo3 is involved in proton translocation
- Proton uptake controls electron transfer in cytochrome c oxidase
- Electron transfer between hemes in mammalian cytochrome c oxidase
- Mechanism of the electron transfer catalyst DsbB from Escherichia coli
