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

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 si...

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Published in:IUBMB life 2015-02, Vol.67 (2), p.98-109
Main Authors: Ascenzi, Paolo, Coletta, Massimo, Wilson, Michael T., Fiorucci, Laura, Marino, Maria, Polticelli, Fabio, Sinibaldi, Federica, Santucci, Roberto
Format: Article
Language:English
Subjects:
Animals
Apoptosis
Cardiolipins - metabolism
cardiolipin–cytochrome c complex
Cytochromes c - metabolism
Electron Transport
Heme - metabolism
Humans
Inactivation, Metabolic
Multiprotein Complexes - metabolism
Myoglobin - metabolism
nitrite reductase activity
Nitrite Reductases - metabolism
Oxidation-Reduction
peroxidase activity
peroxynitrite detoxification
Peroxynitrous Acid - metabolism
Peroxynitrous Acid - pharmacokinetics
Protein Carbonylation
redox properties
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Summary: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. © 2015 IUBMB Life, 67(2):98–109, 2015
ISSN:1521-6543
1521-6551
DOI:10.1002/iub.1350