Journal
BIOCHEMISTRY
Volume 55, Issue 3, Pages 407-428Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.biochem.5b01385
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Funding
- Agencia Nacional de Investigacion e Innovacion [FCE_2014_104233]
- Universidad de la Republica (CSIC-UdelaR)
- National Institutes of Health [RO1 AI095173]
- ANPCyT [PICT 2010-070, 2011-1249]
- UBACyT [20020130100206BA]
- Programa de Desarrollo de Ciencias Basicas (PEDECIBA)
- Centro de Biologia Estructural del Mercosur (CeBEM)
- CONICET
- Ridaline and Bidden through Fundacion Manuel Perez
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Cytochrome c (cyt c) is a cationic hemoprotein of similar to 100 amino acid residues that exhibits exceptional functional versatility. While its primary function is electron transfer in the respiratory chain, cyt c is also recognized as a key component of the intrinsic apoptotic pathway, the mitochondrial oxidative protein folding machinery, and presumably as a redox sensor in the cytosol, along with other reported functions. Transition to alternative conformations and gain-of-peroxidase activity are thought to further enable the multiple functions of cyt c and its translocation across cellular compartments. In vitro, direct interactions of cyt c with cardiolipin, post-translational modifications such as tyrosine nitration, phosphorylation, methionine sulfoxidation, mutations, and even fine changes in electrical fields lead to a variety of conformational states that may be of biological relevance. The identification of these alternative conformations and the elucidation of their functions in vivo continue to be a major challenge. Here, we unify the knowledge of the structural flexibility of cyt c that supports functional moonlighting and review biochemical and immunochemical evidence confirming that cyt c undergoes conformational changes during normal and altered cellular homeostasis.
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