HYDROGEN PEROXIDE-INUDUCED GAIN OF PEROXIDASE ACTIVITYOF CYTOCHROME C UPON PHOSPHATE-MEDIATED BINDING TO ZWITTERIONIC LIPIDS: IMPLICATIONS FOR APOPTOSIS

DAIANA ANDREA CAPDEVILA; WALDEMAR MARMISOLLÉ; FLORENCIA TOMASINA; VERONICA DEMICHELI; RAFAEL RADI; DANIEL MURGIDA

Chascomus

Congreso; IV Latin American Meeting on Biological Inorganic Chemistry; 2014

Society of Biological Inorganic Chemistry

Cytochrome c (Cyt-c) has been shown to participate in cardiolipin (CL) oxidation and, therefore, in mitochondrial membrane permeabilization during the early events of apoptosis. The gain of peroxidatic activity has been ascribed to CL/Cyt-c interactions which, nevertheless, are also ubiquitous in non-apoptotic cells, thereby posing the question of which is the triggering event. In a previous report, we observed that the cationic protein Cyt-c is able to interact electrostatically with the main lipid components of the mitochondrial membranes, the zwitterionic lipids phosphatidylethanolamine (PE) and phosphatidylcholine (PC), through mediating phosphate anions that interact specifically with amino groups in the surfaces of the protein and the membrane models1.