In contrast to earlier unpublished observations in this laboratory, it was reported by other workers that the modification of proteins by peroxynitrite leads to the conversion of some amino acid residues to carbonyl derivatives. The discrepancy between our results and those reported earlier has been resolved. It is due to the failure of the other workers to take into account the contribution of light scattering in their spectrophotometric measurements of protein carbonyl content. Nevertheless, in view of the fact that the carbonyl content of proteins is a widely accepted measure of oxidative stress and has been used as a marker of oxidative damage during aging and in many diseases, we investigated further the modification of proteins by peroxynitrite. We confirmed our earlier findings that the oxidation of methionine residues of glutamine synthetase by peroxynitrite is strongly inhibited by physiological concentrations of carbon dioxide, and that the nitration of tyrosine residues is almost completely dependent on the presence of carbon dioxide. We confirmed also that peroxynitrite does not generate significant amounts of protein carbonyl groups at physiological concentrations of hydrogen ion and carbon dioxide. However, the dependence of these reactions on carbon dioxide varies with the concentration of hydrogen ion. These results emphasize the importance of controlling the hydrogen ion concentration and carbon dioxide levels of reaction mixtures in vitro in studies designed to determine the modification of proteins by peroxynitrite. They show further that only marginal levels of protein carbonyl are generated by peroxynitrite under any of the experimental conditions examined. It is therefore unlikely that peroxynitrite contributes significantly to the increase in levels of protein carbonyl groups observed during aging and in various diseases.
| Noda, Yasuko; Berlett, Barbara S; Stadtman, Earl R et al. (2007) Identification of enzymes and regulatory proteins in Escherichia coli that are oxidized under nitrogen, carbon, or phosphate starvation. Proc Natl Acad Sci U S A 104:18456-60 |
| Tanaka, Mikiei; Chock, P Boon; Stadtman, Earl R (2007) Oxidized messenger RNA induces translation errors. Proc Natl Acad Sci U S A 104:66-71 |
| Miyoshi, Noriyuki; Oubrahim, Hammou; Chock, P Boon et al. (2006) Age-dependent cell death and the role of ATP in hydrogen peroxide-induced apoptosis and necrosis. Proc Natl Acad Sci U S A 103:1727-31 |
| Khan, Mohammed A S; Chock, P Boon; Stadtman, Earl R (2005) Knockout of caspase-like gene, YCA1, abrogates apoptosis and elevates oxidized proteins in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 102:17326-31 |
| Stadtman, Earl R; Van Remmen, Holly; Richardson, Arlan et al. (2005) Methionine oxidation and aging. Biochim Biophys Acta 1703:135-40 |
| Lee, Byung Cheon; Lee, Yong Kwon; Lee, Ho-Joung et al. (2005) Cloning and characterization of antioxidant enzyme methionine sulfoxide-S-reductase from Caenorhabditis elegans. Arch Biochem Biophys 434:275-81 |
| Stadtman, Earl R; Arai, Hirofumi; Berlett, Barbara S (2005) Protein oxidation by the cytochrome P450 mixed-function oxidation system. Biochem Biophys Res Commun 338:432-6 |
| Oubrahim, Hammou; Wang, Jun; Stadtman, Earl R et al. (2005) Molecular cloning and characterization of murine caspase-12 gene promoter. Proc Natl Acad Sci U S A 102:2322-7 |
| Arai, Hirofumi; Berlett, Barbara S; Chock, P Boon et al. (2005) Effect of bicarbonate on iron-mediated oxidation of low-density lipoprotein. Proc Natl Acad Sci U S A 102:10472-7 |
| Khan, Mohammed A S; Oubrahim, Hammou; Stadtman, Earl R (2004) Inhibition of apoptosis in acute promyelocytic leukemia cells leads to increases in levels of oxidized protein and LMP2 immunoproteasome. Proc Natl Acad Sci U S A 101:11560-5 |
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