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Biochim Biophys Acta. 2013 Nov;1830(11):4981-9. doi: 10.1016/j.bbagen.2013.07.002. Epub 2013 Jul 13.

Inhibition of peroxisomal hydroxypyruvate reductase (HPR1) by tyrosine nitration.

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  • 1Departamento de Bioquímica, Biología Celular y Molecular de Plantas, Estación Experimental del Zaidín (EEZ), CSIC, Apartado 419, E-18080 Granada, Spain. Electronic address:



Protein tyrosine nitration is a post-translational modification (PTM) mediated by nitric oxide-derived molecules. Peroxisomes are oxidative organelles in which the presence of nitric oxide (NO) has been reported.


We studied peroxisomal nitroproteome of pea leaves by high-performance liquid chromatography with tandem mass spectrometry (LC-MS/MS) and proteomic approaches.


Proteomic analysis of peroxisomes from pea leaves detected a total of four nitro-tyrosine immunopositive proteins by using an antibody against nitrotyrosine. One of these proteins was found to be the NADH-dependent hydroxypyruvate reductase (HPR). The in vitro nitration of peroxisomal samples caused a 65% inhibition of HPR activity. Analysis of recombinant peroxisomal NADH-dependent HPR1 activity from Arabidopsis in the presence of H2O2, NO, GSH and peroxynitrite showed that the ONOO(-) molecule caused the highest inhibition of activity (51% at 5mM SIN-1), with 5mM H2O2 having no inhibitory effect. Mass spectrometric analysis of the nitrated recombinant HPR1 enabled us to determine that, among the eleven tyrosine present in this enzyme, only Tyr-97, Tyr-108 and Tyr-198 were exclusively nitrated to 3-nitrotyrosine by peroxynitrite. Site-directed mutagenesis confirmed Tyr198 as the primary site of nitration responsible for the inhibition on the enzymatic activity by peroxynitrite.


These findings suggest that peroxisomal HPR is a target of peroxynitrite which provokes a loss of function.


This is the first report demonstrating the peroxisomal NADH-dependent HPR activity involved in the photorespiration pathway is regulated by tyrosine nitration, indicating that peroxisomal NO metabolism may contribute to the regulation of physiological processes under no-stress conditions.

© 2013.


3-morpholinosydnonimine; GSH; GSNO; HPR; Hydroxypyruvate reductase; NO; Nitration; Nitric oxide; Nitro-proteome; ONOO(−); PTM; Peroxisome; Peroxynitrite; RNS; S-nitrosoglutathione; SIN-1; hydroxypyruvate reductase; nitric oxide; peroxynitrite; post-translational modification; reactive nitrogen species; reduced glutathione

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