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

AuthorsGarcía-Heredia, José M. ; Díaz-Moreno, Irene ; Díaz-Quintana, Antonio; Orzáez, Mar; Navarro, José A. ; Hervás, Manuel ; Rosa, Miguel A. de la
KeywordsMitochondrial respiration
Electron transfer
Cytochrome c oxidase
Tyrosine nitration
Caspase-9 activation
Post-translational modification
Cytochrome c
Issue Date2012
CitationFEBS Letters 586: 154- 158 (2012)
AbstractUnder 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.
Identifiersdoi: 10.1016/j.febslet.2011.12.007
issn: 0014-5793
Appears in Collections:(IBVF) Artículos
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