Catalase catalyzes nitrotyrosine formation from sodium azide and hydrogen peroxide |
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| Authors: | Keiki Ogino Norio Kodama Madoka Nakajima Akihiro Yamada Hiroyuki Nakamura Hirohumi Nagase Daikai Sadamitsu Takeshi Maekawa |
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| Institution: |
a Department of Environmental and Preventative Medicine, Graduate School of Medical Science, Kanazawa University, Kanazawa, Japan
b Department of Emergency and Critical Care, Yamaguchi University School of Medicine, Kogushi Ube, Japan |
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| Abstract: | Sodium azide (NaN3) is known as an inhibitor of catalase, and a nitric oxide (NO) donor in the presence of catalase and H2O2. We showed here that catalase-catalyzed oxidation of NaN3 can generate reactive nitrogen species which contribute to tyrosine nitration in the presence of H2O2. The formation of free-tyrosine nitration and protein-bound tyrosine nitration by the NaN3/catalase/H2O2 system showed a maximum level at pH 6.0. Free-tyrosine nitration induced by peroxynitrite was inhibited by ethanol and dimethyl-sulfoxide (DMSO), and augmented by superoxide dismutase (SOD). However, free-tyrosine nitration induced by the NaN3/catalase/H2O2 system was not affected by ethanol, DMSO and SOD. NO-2 and NO donating agents did not affect free-tyrosine nitration by the NaN3/catalase/H2O2 system. The reaction of NaN3 with hydroxyl radical generating system showed free-tyrosine nitration, but no formation of nitrite and nitrate. The generation of nitrite (NO-2) and nitrate (NO-3) by the NaN3/catalase/H2O2 system was maximal at pH 5.0. These results suggested that the oxidation of NaN3 by the catalase/H2O2 system generates unknown peroxynitrite-like reactive nitrogen intermediates, which contribute to tyrosine nitration. |
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