The interaction of cytochrome C with phospholipids. A pulse-radiolysis study.
AffiliationPaterson Laboratories, Christie Hospital and Holt Radium Institute, Manchester.
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AbstractThe reactions of the hydrated electron (eaq-), produced during pulse radiolysis, have been used to study the binding of phosphatidyl choline (PC), phosphatidyl serine (PS), phosphatidyl ethanolamine (PE), and phosphatidyl inositol (PI) vesicles with horse-heart cytochrome C. An interaction could only be detected between cytochrome C and either PS or PI. An apparent equivalence point in the binding was reached for both phospholipids at a molar ratio of phospholipid : protein of 6 : 1. At this point, the reactivity of (eaq-) towards the cytochrome C was very markedly reduced. Indeed, the rate of disappearance of (eaq-) under such conditions was the same as the rate of eaq- disappearance in triply-distilled water. The inclusion of cholesterol at a molar ratio of 1 : 1 within the phospholipid vesicles changed the stoichiometry of the interaction. Evidence that protonated epsilon-amino groups of lysine residues are involved in the interaction is presented. Possible models for the complexes formed are discussed.
CitationThe interaction of cytochrome C with phospholipids. A pulse-radiolysis study. 1978, 33 (2):151-62 Int. J. Radiat. Biol. Relat. Stud. Phys. Chem. Med.
JournalInternational Journal of Radiation Biology and Related studies in Physics, Chemistry, and Medicine
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