Reconstitution of cytochrome bc1 complex into lipid vesicles and the restoration of uncoupler sensitivity

AbstractBeef heart mitochondrial bc1 complex (ubiquinone—cytochrome c oxidoreductase) has been assayed by its ability to catalyse the reaction of duroquinol reduction of ferricytochrome c. When the isolated complex is reincorporated into lipid vesicles, the enzyme-catalysed electron transfer rate becomes uncoupler-sensitive. Initial experiments suggest that a protonmotive force is generated across the vesicles when electron transfer is initiated. Both ΔΨ and ΔpH components of this protonmotive force then influence an internal rate constant of the bc1 complex