Functions of the hydrophilic channels in protonmotive cytochrome c oxidase
Author(s) -
Peter R. Rich,
Amandine Maréchal
Publication year - 2013
Publication title -
journal of the royal society interface
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.655
H-Index - 139
eISSN - 1742-5689
pISSN - 1742-5662
DOI - 10.1098/rsif.2013.0183
Subject(s) - proton , ion channel , cytochrome c oxidase , biophysics , cytochrome , chemistry , electron transport chain , cytochrome c , membrane potential , physics , biology , biochemistry , mitochondrion , enzyme , receptor , quantum mechanics
The structures and functions of hydrophilic channels in electron-transferring membrane proteins are discussed. A distinction is made between proton channels that can conduct protons and dielectric channels that are non-conducting but can dielectrically polarize in response to the introduction of charge changes in buried functional centres. Functions of the K, D and H channels found in A1-type cytochrome c oxidases are reviewed in relation to these ideas. Possible control of function by dielectric channels and their evolutionary relation to proton channels is explored.
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