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.

Ascenzi, P., Coletta, M., Wilson, M., Fiorucci, L., Marino, M., Polticelli, F., et al. (2015). Cardiolipin-cytochrome c complex: Switching cytochrome c from an electron-transfer shuttle to a myoglobin- and a peroxidase-like heme-protein. IUBMB LIFE, 67(2), 98-109 [10.1002/iub.1350].

Cardiolipin-cytochrome c complex: Switching cytochrome c from an electron-transfer shuttle to a myoglobin- and a peroxidase-like heme-protein

COLETTA, MASSIMILIANO;FIORUCCI, LAURA;SINIBALDI, FEDERICA;SANTUCCI, ROBERTO
2015

Abstract

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.
Pubblicato
Rilevanza internazionale
Articolo
Esperti anonimi
Settore BIO/10
English
Con Impact Factor ISI
apoptosis; cardiolipin-cytochrome c complex; nitrite reductase activity; peroxidase activity; peroxynitrite detoxification; redox properties; Animals; Apoptosis; Cardiolipins; Cytochromes c; Electron Transport; Heme; Humans; Inactivation, Metabolic; Multiprotein Complexes; Myoglobin; Nitrite Reductases; Oxidation-Reduction; Peroxynitrous Acid; Protein Carbonylation
Ascenzi, P., Coletta, M., Wilson, M., Fiorucci, L., Marino, M., Polticelli, F., et al. (2015). Cardiolipin-cytochrome c complex: Switching cytochrome c from an electron-transfer shuttle to a myoglobin- and a peroxidase-like heme-protein. IUBMB LIFE, 67(2), 98-109 [10.1002/iub.1350].
Ascenzi, P; Coletta, M; Wilson, M; Fiorucci, L; Marino, M; Polticelli, F; Sinibaldi, F; Santucci, R
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2108/172302
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