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Free Radic Biol Med. 2009 Jun 1;46(11):1439-53. doi: 10.1016/j.freeradbiomed.2009.03.004. Epub 2009 Mar 12.

Cytochrome c/cardiolipin relations in mitochondria: a kiss of death.

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  • 1Center for Free Radical and Antioxidant Health, Pittsburgh, PA 15219, USA. kagan@pitt.edu

Abstract

Recently, phospholipid peroxidation products gained a reputation as key regulatory molecules and participants in oxidative signaling pathways. During apoptosis, a mitochondria-specific phospholipid, cardiolipin (CL), interacts with cytochrome c (cyt c) to form a peroxidase complex that catalyzes CL oxidation; this process plays a pivotal role in the mitochondrial stage of the execution of the cell death program. This review is focused on redox mechanisms and essential structural features of cyt c's conversion into a CL-specific peroxidase that represent an interesting and maybe still unique example of a functionally significant ligand change in hemoproteins. Furthermore, specific characteristics of CL in mitochondria--its asymmetric transmembrane distribution and mechanisms of collapse, the regulation of its synthesis, remodeling, and fatty acid composition--are given significant consideration. Finally, new concepts in drug discovery based on the design of mitochondria-targeted inhibitors of cyt c/CL peroxidase and CL peroxidation with antiapoptotic effects are presented.

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