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• W2044272839 startingPage "4963" @default.
• W2044272839 abstract "Membrane protein complexes can support both the generation and utilisation of a transmembrane electrochemical proton potential ('proton-motive force'), either by transmembrane electron transfer coupled to protolytic reactions on opposite sides of the membrane or by transmembrane proton transfer. Here we provide the first evidence that both of these mechanisms are combined in the case of a specific respiratory membrane protein complex, the dihaem-containing quinol:fumarate reductase (QFR) of Wolinella succinogenes, so as to facilitate transmembrane electron transfer by transmembrane proton transfer. We also demonstrate the non-functionality of this novel transmembrane proton transfer pathway ('E-pathway') in a variant QFR where a key glutamate residue has been replaced. The 'E-pathway', discussed on the basis of the 1.78-Angstrom-resolution crystal structure of QFR, can be concluded to be essential also for the viability of pathogenic epsilon-proteobacteria such as Helicobacter pylori and is possibly relevant to proton transfer in other dihaem-containing membrane proteins, performing very different physiological functions." @default.
• W2044272839 created "2016-06-24" @default.
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• W2044272839 date "2006-10-05" @default.
• W2044272839 modified "2023-09-27" @default.
• W2044272839 title "Evidence for transmembrane proton transfer in a dihaem-containing membrane protein complex" @default.
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• W2044272839 doi "https://doi.org/10.1038/sj.emboj.7601361" @default.
• W2044272839 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1618101" @default.
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