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• W2040797588 startingPage "96" @default.
• W2040797588 abstract "Cytochrome c oxidase (CcO) reconstituted into phospholipid vesicles and subject to a membrane potential, exhibits different characteristics than the free enzyme, with respect to effects of mutations, pH, inhibitors, and native structural differences between CcO from different species. The results indicate that the membrane potential influences the conformation of CcO and the direction of proton movement in the exit path. The importance of the protein structure above the hemes in proton exit, back leak and respiratory control is discussed." @default.
• W2040797588 created "2016-06-24" @default.
• W2040797588 creator A5061957865 @default.
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• W2040797588 date "2002-09-01" @default.
• W2040797588 modified "2023-09-29" @default.
• W2040797588 title "Influence of structure, pH and membrane potential on proton movement in cytochrome oxidase" @default.
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• W2040797588 doi "https://doi.org/10.1016/s0005-2728(02)00261-x" @default.
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