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- W2054223556 abstract "Aerobic life is based on a molecular machinery that utilizes oxygen as a terminal electron sink. The membrane-bound cytochrome c oxidase (CcO) catalyzes the reduction of oxygen to water in mitochondria and many bacteria. The energy released in this reaction is conserved by pumping protons across the mitochondrial or bacterial membrane, creating an electrochemical proton gradient that drives production of ATP. A crucial question is how the protons pumped by CcO are prevented from flowing backwards during the process. Here, we show by molecular dynamics simulations that the conserved glutamic acid 242 near the active site of CcO undergoes a protonation state-dependent conformational change, which provides a valve in the pumping mechanism. The valve ensures that at any point in time, the proton pathway across the membrane is effectively discontinuous, thereby preventing thermodynamically favorable proton back-leakage while maintaining an overall high efficiency of proton translocation. Suppression of proton leakage is particularly important in mitochondria under physiological conditions, where production of ATP takes place in the presence of a high electrochemical proton gradient." @default.
- W2054223556 created "2016-06-24" @default.
- W2054223556 creator A5010061575 @default.
- W2054223556 creator A5059945365 @default.
- W2054223556 creator A5063740635 @default.
- W2054223556 creator A5091246390 @default.
- W2054223556 date "2008-04-29" @default.
- W2054223556 modified "2023-09-30" @default.
- W2054223556 title "Glutamic acid 242 is a valve in the proton pump of cytochrome <i>c</i> oxidase" @default.
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- W2054223556 doi "https://doi.org/10.1073/pnas.0800770105" @default.
- W2054223556 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2359812" @default.
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