Open AccessElectron – proton coupling in cytochrome c studied using protein variants
Author(s) -
GAO Yuan,
McLENDON George,
PIELAK Gary J.,
WILLIAMS Robert J. P.
Publication year - 1992
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1992.tb16642.x
Subject(s) - redox , cytochrome c , proton , cytochrome , gating , chemistry , electron transport chain , coupling (piping) , cytochrome c1 , cytochrome b , crystallography , photochemistry , chemical physics , coenzyme q – cytochrome c reductase , biophysics , physics , materials science , biochemistry , mitochondrion , biology , inorganic chemistry , enzyme , quantum mechanics , gene , metallurgy , mitochondrial dna
An NMR study of the cytochrome c variant Asn52Ile is used to show how the redox state change in native cytochrome c is coupled to a rearrangement of a proton network which runs through the cytochrome c molecule. The substitution breaks the H‐bond network and removes the coupling. The uncovering of this putative proton channel and the connection of changes to it with redox state changes of the iron centre of the protein allows a possible description of the way in which redox energy state changes can be coupled to energisation and gating of protons in membranes.