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

doi:10.1080/10715760100301241

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 journal › Article › peer-review

25 Citations (Scopus)

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. 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 language	English
Pages (from-to)	735-747
Number of pages	13
Journal	Free Radical Research
Volume	35
Issue number	6
DOIs	https://doi.org/10.1080/10715760100301241
Publication status	Published - 2001
Externally published	Yes

Keywords

Azidyl radical
Catalase
Nitrotyrosine
Peroxynitrite
Sodium azide

ASJC Scopus subject areas

Biochemistry

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10.1080/10715760100301241

Cite this

@article{cf7445c374e84bce887ddc42fe7eb1f9,

title = "Catalase catalyzes nitrotyrosine formation from sodium azide and hydrogen peroxide",

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. 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.",

keywords = "Azidyl radical, Catalase, Nitrotyrosine, Peroxynitrite, Sodium azide",

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

note = "Funding Information: This work was supported in part by a Grant-in-Aid from the Ministry of Education, Science and Culture. We express many thanks to Mrs Hitomi lkernoto of Yamaguchi University School of Medicine for her helpful assistance.",

year = "2001",

doi = "10.1080/10715760100301241",

language = "English",

volume = "35",

pages = "735--747",

journal = "Free Radical Research",

issn = "1071-5762",

publisher = "Informa Healthcare",

number = "6",

}

TY - JOUR

T1 - Catalase catalyzes nitrotyrosine formation from sodium azide and hydrogen peroxide

AU - Ogino, Keiki

AU - Kodama, Norio

AU - Nakajima, Madoka

AU - Yamada, Akihiro

AU - Nakamura, Hiroyuki

AU - Nagase, Hirohumi

AU - Sadamitsu, Daikai

AU - Maekawa, Takeshi

N1 - Funding Information: This work was supported in part by a Grant-in-Aid from the Ministry of Education, Science and Culture. We express many thanks to Mrs Hitomi lkernoto of Yamaguchi University School of Medicine for her helpful assistance.

PY - 2001

Y1 - 2001

N2 - 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.

AB - 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.

KW - Azidyl radical

KW - Catalase

KW - Nitrotyrosine

KW - Peroxynitrite

KW - Sodium azide

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U2 - 10.1080/10715760100301241

DO - 10.1080/10715760100301241

M3 - Article

C2 - 11811525

AN - SCOPUS:0035692283

SN - 1071-5762

VL - 35

SP - 735

EP - 747

JO - Free Radical Research

JF - Free Radical Research

IS - 6

ER -

Catalase catalyzes nitrotyrosine formation from sodium azide and hydrogen peroxide

Abstract

Keywords

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