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A mechano‐chemical model for energy transduction in cytochrome c oxidase: the work of a Maxwell's god
Author(s) -
Xavier António V
Publication year - 2002
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(02)03692-x
Subject(s) - cytochrome c oxidase , chemistry , redox , biophysics , cytochrome , chemical energy , coupling (piping) , work (physics) , chemical physics , enzyme , biochemistry , physics , materials science , thermodynamics , biology , inorganic chemistry , organic chemistry , metallurgy
Cytochrome c 3 has a central role in the energetics of Desulfovibrio sp., where it performs an electroprotonic energy transduction step. This process uses a network of cooperativities, largely based on anti‐Coulomb components, resulting from a mechano‐chemical energy coupling mechanism. This mechanism provides a model coherent with the data available for the redox chemistry of haem a of cytochrome c oxidase and its link to the activation of protons. A crucial feature of the model is an anti‐Coulomb effect that sets the stage for a molecular ratchet, ensuring vectoriality for the redox‐driven localised movement of protons across the membrane, against an electrochemical gradient.