Journal
IUBMB LIFE
Volume 67, Issue 2, Pages 98-109Publisher
WILEY
DOI: 10.1002/iub.1350
Keywords
cardiolipin-cytochrome c complex; redox properties; nitrite reductase activity; peroxidase activity; peroxynitrite detoxification; apoptosis
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Funding
- Ministero dell'Istruzione, dell'Universita e della Ricerca of Italy [PRIN 20109MXHMR_001, FIRB RBNE03PX83]
- Universita Roma Tre (CLA)
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Cytochrome c (cytc) is a small heme-protein located in the space between the inner and the outer membrane of the mitochondrion that transfers electrons from cytc-reductase to cytc-oxidase. The hexa-coordinated heme-Fe atom of cytc displays a very low reactivity toward ligands and does not exhibit significant catalytic properties. However, upon cardiolipin (CL) binding, cytc achieves ligand binding and catalytic properties reminiscent of those of myoglobin and peroxidase. In particular, the peroxidase activity of the cardiolipin-cytochrome c complex (CL-cytc) is critical for the redistribution of CL from the inner to the outer mitochondrial membranes and is essential for the execution and completion of the apoptotic program. On the other hand, the capability of CL-cytc to bind NO and CO and the heme-Fe-based scavenging of reactive nitrogen and oxygen species may affect apoptosis. Here, the ligand binding and catalytic properties of CL-cytc are analyzed in parallel with those of CL-free cytc, myoglobin, and peroxidase to dissect the potential mechanisms of CL in modulating the pro- and anti-apoptotic actions of cytc. (c) 2015 IUBMB Life, 67(2):98-109, 2015
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