Abstract
AbstractThe structure and the electron‐transfer of cytochrome c binding on the anionic lipid vesicles were analyzed by electrochemical and various spectroscopic methods. It was found that upon binding to anionic lipid membrane, the formal potential of cytochrome c shifted 30 mV negatively indicating an easier redox interaction than that in its native state. This is due to the local alteration of the coordination and the heme crevice. The structural perturbation in which a molten globule‐like state is formed during binding to anionic lipid vesicles is more important. This study may help to understand the mechanism of the electron‐transfer reactions of cytochrome c at the mitochondrial membrane.
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