Association of cytochrome c with anionic membranes involved both electrostatic and hydrophobic interactions and their relative contributions depended on the physical state of the membrane and the redox state of cytochrome c. Hydrophobic interaction was favored by the membranes in gel phase, by the membranes with a large curvature, and by the membranes with a high surface charge density. Ferrocytochrome c was less dissociable by NaCl than ferricytochrome c suggesting that a lower protein stability is beneficial for hydrophobic interaction. Hydrophobic interaction induced larger structural perturbations on cytochrome c as monitored by the loss of the Fe-Met bond and by the increase in the distance between heme and Trp-59. When bound to anionic membranes, spin-labeled cytochrome c showed an electron paramagnetic resonance spectrum with two or more components, providing a direct evidence for multiple conformations of bound cytochrome c.
|Original language||English (US)|
|Number of pages||7|
|Journal||Bulletin of the Korean Chemical Society|
|State||Published - Apr 20 2000|
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