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• W2045542314 endingPage "663" @default.
• W2045542314 startingPage "659" @default.
• W2045542314 abstract "The proton-pumping NADH:ubiquinone oxidoreductase couples the transfer of electrons from NADH to ubiquinone with the translocation of protons across the membrane. This process is suggested to be accompanied by conformational changes of the enzyme that may be monitored by redox-induced FT-IR difference spectroscopy. Signals observed in the amide I range are partially attributed to local rearrangements that occur as an electrostatic response to the redox reactions of the FeS clusters. In addition, conformational changes can be reported that depend on pH and at the same time can be perturbed by site-directed mutagenesis of residue E67 on subunit B (the bacterial homologue of the mitochondrial PSST subunit). This residue is located in the vicinity of the cluster N2. Re-evaluating these previous data we here discuss a mechanism, by which the redox reaction of N2 induces conformational changes possibly leading to proton translocation." @default.
• W2045542314 created "2016-06-24" @default.
• W2045542314 creator A5000422071 @default.
• W2045542314 creator A5025917396 @default.
• W2045542314 date "2010-06-01" @default.
• W2045542314 modified "2023-10-04" @default.
• W2045542314 title "Redox-induced conformational changes within the Escherichia coli NADH ubiquinone oxidoreductase (complex I): An analysis by mutagenesis and FT-IR spectroscopy" @default.
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• W2045542314 doi "https://doi.org/10.1016/j.bbabio.2010.03.002" @default.
• W2045542314 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20214873" @default.
• W2045542314 hasPublicationYear "2010" @default.
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