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- W2092035009 abstract "Na + -NQR is a unique energy-transducing complex, widely distributed among marine and pathogenic bacteria. It converts the energy from the oxidation of NADH and the reduction of quinone into an electrochemical Na + -gradient that can provide energy for the cell. Na + -NQR is not homologous to any other respiratory protein but is closely related to the RNF complex. In this review we propose that sodium pumping in Na + -NQR is coupled to the redox reactions by a novel mechanism, which operates at multiple sites, is indirect and mediated by conformational changes of the protein. This article is part of a Special Issue entitled: 17th European Bioenergetics Conference (EBEC 2012). ► Na + -NQR is a respiratory enzyme essential in the metabolism of many marine and pathogenic bacteria. ► Na + -NQR selectively translocates only Na+ across the cell membrane. ► Na + -NQR has five redox cofactors: FAD, 2Fe-2S center, two covalently bound FMN's and riboflavin. ► Coupling of Na + transport to redox reactions is indirect. ► Coupling is likely mediated by conformational changes." @default.
- W2092035009 created "2016-06-24" @default.
- W2092035009 creator A5059232759 @default.
- W2092035009 creator A5090976040 @default.
- W2092035009 date "2012-10-01" @default.
- W2092035009 modified "2023-09-23" @default.
- W2092035009 title "Insights into the mechanism of electron transfer and sodium translocation of the Na+-pumping NADH:quinone oxidoreductase" @default.
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- W2092035009 doi "https://doi.org/10.1016/j.bbabio.2012.03.017" @default.
- W2092035009 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8172247" @default.
- W2092035009 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22465856" @default.
- W2092035009 hasPublicationYear "2012" @default.
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