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

Paolo Ascenzi, Massimo Coletta, Michael T. Wilson, Laura Fiorucci, Maria Marino, Fabio Polticelli, Federica Sinibaldi, Roberto Santucci

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Pages (from-to)98-109
Number of pages12
JournalIUBMB Life
Volume67
Issue number2
DOIs
Publication statusPublished - Feb 1 2015

Keywords

  • apoptosis
  • cardiolipin-cytochrome c complex
  • nitrite reductase activity
  • peroxidase activity
  • peroxynitrite detoxification
  • redox properties

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Clinical Biochemistry
  • Molecular Biology
  • Genetics

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