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Specific nitration of tyrosines 46 and 48 makes cytochrome c assemble a non-functional apoptosome

AutorGarcía-Heredia, José M. ; Díaz-Moreno, Irene ; Díaz-Quintana, Antonio; Orzáez, Mar; Navarro, José A. ; Hervás, Manuel ; Rosa, Miguel A. de la
Palabras claveMitochondrial respiration
Electron transfer
Cytochrome c oxidase
Tyrosine nitration
Caspase-9 activation
Post-translational modification
RNOS
Cytochrome c
Apoptosome
Fecha de publicación2012
EditorElsevier
CitaciónFEBS Letters 586: 154- 158 (2012)
ResumenUnder nitroxidative stress, a minor fraction of cytochrome c can be modified by tyrosine nitration. Here we analyze the specific effect of nitration of tyrosines 46 and 48 on the dual role of cytochrome c in cell survival and cell death. Our findings reveal that nitration of these two solvent-exposed residues has a negligible effect on the rate of electron transfer from cytochrome c to cytochrome c oxidase, but impairs the ability of the heme protein to activate caspase-9 by assembling a non-functional apoptosome. It seems that cytochrome c nitration under cellular stress counteracts apoptosis in light of the small amount of modified protein. We conclude that other changes such as increased peroxidase activity prevail and allow the execution of apoptosis. © 2011 Elsevier Ltd. All rights reserved.
URIhttp://hdl.handle.net/10261/95810
DOI10.1016/j.febslet.2011.12.007
Identificadoresdoi: 10.1016/j.febslet.2011.12.007
issn: 0014-5793
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