Premium
Cardiolipin–cytochrome c complex: Switching cytochrome c from an electron‐transfer shuttle to a myoglobin‐ and a peroxidase‐like heme‐protein
Author(s) -
Ascenzi Paolo,
Coletta Massimo,
Wilson Michael T.,
Fiorucci Laura,
Marino Maria,
Polticelli Fabio,
Sinibaldi Federica,
Santucci Roberto
Publication year - 2015
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1002/iub.1350
Subject(s) - cardiolipin , cytochrome c , chemistry , cytochrome c peroxidase , peroxidase , heme , cytochrome c oxidase , myoglobin , hemeprotein , mitochondrion , biochemistry , membrane , enzyme , phospholipid
Cytochrome c (cyt c ) is a small heme‐protein located in the space between the inner and the outer membrane of the mitochondrion that transfers electrons from cyt c ‐reductase to cyt c ‐oxidase. The hexa‐coordinated heme‐Fe atom of cyt c displays a very low reactivity toward ligands and does not exhibit significant catalytic properties. However, upon cardiolipin (CL) binding, cyt c 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–cyt c ) 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–cyt c 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–cyt c are analyzed in parallel with those of CL‐free cyt c , myoglobin, and peroxidase to dissect the potential mechanisms of CL in modulating the pro‐ and anti‐apoptotic actions of cyt c . © 2015 IUBMB Life, 67(2):98–109, 2015