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- W2019469507 abstract "Significance The transmembrane proton gradient is the primary source of cellular energy. Cytochrome c oxidase pumps protons uphill across the membrane using the energy released by the reduction of O 2 . Proton transport requires that residues change their proton affinity during the reaction cycle. Calculation of proton binding identifies a cluster of residues that bind and release a proton on each reduction of the active site. These residues can constitute a proton loading site. The heme propionic acids play the central role in proton loading. If the propionic acid proton affinity is too low, no protons will be loaded. The same proton-pumping mechanism can be used for each of the four redox steps carried out in the reaction cycle." @default.
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- W2019469507 date "2014-08-11" @default.
- W2019469507 modified "2023-09-30" @default.
- W2019469507 title "Characterizing the proton loading site in cytochrome <i>c</i> oxidase" @default.
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- W2019469507 doi "https://doi.org/10.1073/pnas.1407187111" @default.
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