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

► Solvent-exposed tyrosines 46 and 48 of cytochrome c are nitrated in vitro. ► Nitration of cytochrome c does not affect the reaction with cytochrome c oxidase. ► Nitration of cytochrome c impairs its ability to activate caspase-9. Under nitroxidative stress, a minor fraction of cytochrome c can be...

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Veröffentlicht in:	FEBS letters 2012-01, Vol.586 (2), p.154-158
Hauptverfasser:	García-Heredia, José M., Díaz-Moreno, Irene, Díaz-Quintana, Antonio, Orzáez, Mar, Navarro, José A., Hervás, Manuel, De la Rosa, Miguel A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Ac-LEHD-AFC Apaf-1 apoptosis protease-activating factor-1 Apoptosome Apoptosomes - metabolism cardiolipin Caspase-9 activation Caspases - metabolism CcO Cytochrome c Cytochrome c oxidase Cytochromes c - chemistry Cytochromes c - genetics Cytochromes c - metabolism Cytochromes c - physiology Electron transfer Electron Transport - genetics Electron Transport - physiology Enzyme Activation Humans In Vitro Techniques Mitochondrial respiration Mutagenesis, Site-Directed Mutant Proteins - chemistry Mutant Proteins - metabolism Mutant Proteins - physiology N-acetyl-Leu-Glu-His-Asp-(7-amino-4-trifluoromethyl coumarin) Nitrosation - physiology Oxidation-Reduction PC9 Post-translational modification pro-caspase 9 Protein Interaction Domains and Motifs - genetics Protein Interaction Mapping Protein Multimerization - genetics Protein Multimerization - physiology Protein Processing, Post-Translational - physiology reactive nitrogen/oxygen species RNOS Substrate Specificity Tyrosine - chemistry Tyrosine - metabolism Tyrosine nitration
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