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• W2013114026 endingPage "429" @default.
• W2013114026 startingPage "428" @default.
• W2013114026 abstract "The membrane-spanning enzyme known as complex I couples the movement of electrons to that of protons as a way of converting energy. Crystal structures suggest how electron transfer drives proton pumping from afar. Complex I is the first enzyme of the respiratory chain, playing a central role in cellular energy production in the mitochondria by coupling electron transfer between NADH and quinone to proton translocation. This massive complex was the last component of the respiratory chain for which the mechanism and complete structure were unknown. Now the structures of the membrane domain of complex I from Escherichia coli, and of the entire complex I from Thermus thermophilus have been determined. The structures provide strong clues about coupling mechanism: conformational changes at the interface of the two main domains may drive a long α-helix in a piston-like motion, tilting nearby transmembrane helices and resulting in proton translocation." @default.
• W2013114026 created "2016-06-24" @default.
• W2013114026 creator A5079650101 @default.
• W2013114026 date "2010-05-01" @default.
• W2013114026 modified "2023-10-03" @default.
• W2013114026 title "Piston drives a proton pump" @default.
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• W2013114026 doi "https://doi.org/10.1038/465428a" @default.
• W2013114026 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20505714" @default.
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