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Understanding the mechanism of proton movement linked to oxygen reduction in cytochrome c oxidase: lessons from other proteins
Author(s) -
Mills Denise A,
Ferguson-Miller Shelagh
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00392-2
Subject(s) - cytochrome c oxidase , chemistry , electron transport complex iv , cytochrome c1 , cytochrome , electron transfer , proton , oxidase test , biophysics , cytochrome c , electron transport chain , coenzyme q – cytochrome c reductase , chemical physics , biochemistry , photochemistry , enzyme , biology , physics , mitochondrion , quantum mechanics
Cytochrome c oxidase is a large intrinsic membrane protein designed to use the energy of electron transfer and oxygen reduction to pump protons across a membrane. The molecular mechanism of the energy conversion process is not understood. Other proteins with simpler, better resolved structures have been more completely defined and offer insight into possible mechanisms of proton transfer in cytochrome c oxidase. Important concepts that are illustrated by these model systems include the ideas of conformational change both close to and at a distance from the triggering event, and the formation of a transitory water‐linked proton pathway during a catalytic cycle. Evidence for the applicability of these concepts to cytochrome c oxidase is discussed.