Catalase catalyzes nitrotyrosine formation from sodium azide and hydrogen peroxide

Keiki Ogino, Norio Kodama, Madoka Nakajima, Akihiro Yamada, Hiroyuki Nakamura, Hirohumi Nagase, Daikai Sadamitsu, Takeshi Maekawa

Research output: Contribution to journalArticlepeer-review

25 Citations (Scopus)


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. NO2 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 (NO2-) and nitrate (NO3-) 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.

Original languageEnglish
Pages (from-to)735-747
Number of pages13
JournalFree Radical Research
Issue number6
Publication statusPublished - 2001
Externally publishedYes


  • Azidyl radical
  • Catalase
  • Nitrotyrosine
  • Peroxynitrite
  • Sodium azide

ASJC Scopus subject areas

  • Biochemistry


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