Damage of amino acids and proteins induced by nitrogen dioxide, a free radical toxin, in air

Kikugawa, Kiyomi; Kato, Tetsuta; Okamoto, Yutaka

doi:10.1016/0891-5849(94)90039-6

Cited by 83 publications

(46 citation statements)

References 33 publications

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“…Nitration of Tyr may proceed through abstraction of hydrogen by NO 2 followed by addition of NO 2 . 19) Nitrosation of GSH and MOR by NO 2 may proceed through nitration followed by reduction.…”

Section: Discussionmentioning

confidence: 99%

“…The column was eluted with a mobile phase composed of 0.5% (v/v) acetic acid : methanol (29 : 1, v/v) 19) at a flow rate of 1.0 ml/min. The peaks were detected at 280 nm with a detector sensitivity of 0.05.…”

Section: Methodsmentioning

confidence: 99%

“…3-Nitrotyrosine (3-NO 2 Tyr) is produced by reaction of tyrosine (Tyr) with NO 2 , 18,19) ONOO Ϫ /ONOOH 20,21) and other nitrogen oxide species. 22) S-Nitrosoglutathione (GSNO) 23,24) and N-nitrosomorpholine (NMOR) 23,25) are formed by reaction of glutathione (GSH) and morpholine (MOR), respectively, with NO/O 2 .…”

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confidence: 99%

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Effects of Oxygen on the Reactivity of Nitrogen Oxide Species Including Peroxynitrite

Kikugawa

Hiramoto

Ohkawa

2004

Biological & Pharmaceutical Bulletin

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Nitric oxide (NO) has many important biological functions, 1,2) but related nitrogen oxide species including dinitrogen trioxide (N 2 O 3 ), nitrogen dioxide (NO 2 ), and peroxynitrite/peroxynitrous acid (ONOO Ϫ /ONOOH) are known to cause damage to biomolecules such as lipids, proteins, and DNA. There are many reports showing the reactivitiy and decomposition of these nitrogen oxide species in relation to the biologically toxic functions of NO. The reactivity of NO is enhanced by oxygen (O 2 ) through its conversion into the reactive intermediates NO 2 and N 2 O 3 as in Eqs. 1 and 2, and finally into nitrite (NO 2 Ϫ ) as in Eqs. 3 and 4. 3,4) 12) The reactivity and decomposition of ONOO Ϫ are regulated by rapid formation of the CO 2 adduct shown by Eq. 9, [13][14][15][16][17] and the reactivity of this adduct is considered to be important because biological fluids contain a high concentration of CO 2 .Biologically important nitrated and nitrosated compounds are produced by reaction with the nitrogen oxide species. 3-Nitrotyrosine (3-NO 2 Tyr) is produced by reaction of tyrosine (Tyr) 23,24) and N-nitrosomorpholine (NMOR) 23,25) are formed by reaction of glutathione (GSH) and morpholine (MOR), respectively, with NO/O 2 . The reaction of GSH with ONOO Ϫ /ONOOH gives small amounts of GSNO,26,27) whereas the reaction of MOR gives NMOR and N-nitroMOR. 28) GSNO is considered to be a stable NO pool in biological systems, 27,29) and thiol- 30) and metal ion 31)-induced release of NO from nitrosothiols and transnitrosation are known. N-Nitrosamines can be metabolized to form strongly alkylating electrophiles that react with DNA.32) It is conceivable that the presence or absence of O 2 at the locus of generation of nitrogen oxide species can greatly affect the reactivity of the species for the production of nitrated and nitrosated products.The aim of the present study was to compare the reactivity of these nitrogen oxide species for the formation of 3-NO 2 Tyr, GSNO, and NMOR in the presence and absence of O 2 and to determine the effects of O 2 on their reactivity. MATERIALS AND METHODS MaterialsPurified air, NO gas (purity 99.9%), and NO 2 gas (5% in nitrogen gas) were obtained from Nihonsanso Ltd. (Tochigi, Japan), and highly purified nitrogen gas (purity more than 99.9%) was obtained from Taiyo-Toyosanso Ltd. January 2004Biol. Pharm. Bull. 27(1) 17-23 (2004) 17 * To whom correspondence should be addressed. e-mail: kikugawa@ps.toyaku.ac.jp © 2004 Pharmaceutical Society of Japan Effects of Oxygen on the Reactivity of Nitrogen Oxide Species Including PeroxynitriteKiyomi KIKUGAWA,* Kazuyuki HIRAMOTO, and Takumi

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Effects of Oxygen on the Reactivity of Nitrogen Oxide Species Including Peroxynitrite

Kikugawa

Hiramoto

Ohkawa

2004

Biological & Pharmaceutical Bulletin

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“…The sulphur containing amino acids such as methionine and cysteine are more susceptible to oxidation by ROS and are converted to disulphides and methionine sulphoxide [89,90] respectively. However in biological systems, only these two oxidized forms of proteins can be converted back to their native form by two different enzymes namely disulfide reductases and methionine sulfoxide reductases respectively [91][92][93][94]. The ROS mediated attack of different amino acids results in the formation of different oxidation products such as, tryptophan forms nitrotryptophan, kynurenine, formylkynurinine; Phenylalanine forms 2,3-Dihydroxyphenylalanine, 2-, 3-, and 4-hydroxyphenylalanine; Tyrosine forms 3,4-Dihydroxyphenylalanine, tyrosine-tyrosine cross-linkages, Tyr-O-Tyr, cross-linked nitrotyrosine; Histidine forms 2-Oxohistidine, asparagine, aspartic acid; Arginine forms glutamic semialdehyde; Lysine forms a-Aminoadipic semialdehyde; Proline forms 2-Pyrrolidone, 4-and 5-hydroxyproline pyroglutamic acid, glutamic semialdehyde; threonine forms 2-Amino-3-ketobutyric acid; leucine and valine residues form hydroxyl residues [91].…”

Section: Proteinsmentioning

confidence: 99%

Free Radicals: Properties, Sources, Targets, and Their Implication in Various Diseases

2014

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Free radicals and other oxidants have gained importance in the field of biology due to their central role in various physiological conditions as well as their implication in a diverse range of diseases. The free radicals, both the reactive oxygen species (ROS) and reactive nitrogen species (RNS), are derived from both endogenous sources (mitochondria, peroxisomes, endoplasmic reticulum, phagocytic cells etc.) and exogenous sources (pollution, alcohol, tobacco smoke, heavy metals, transition metals,

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“…Tyrosine residues may also react with hydrogen peroxide, yielding 3,4-dihydroxy (dopa) derivative [72,75,76], or bi-tyrosine cross-linked derivatives [73,[77][78][79]. Tryptophan residues are converted to the 2-, 4-, 5-, 6-, or 7-hydroxy derivatives, and also to N-formylkynurenine and kynurenine [72,[80][81][82]. Methionine is readily oxidized to methionine sulfoxide by many different reactive oxygen species [83][84][85].…”

Section: Inactivation Of Enzymes By Modification With Hydrogen Peroxidementioning

confidence: 99%

Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

Hernández

Berenguer-Murcia²,

Rodrigues³

et al. 2012

COC

137

107

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Hydrogen peroxide is a substrate or side-product in many enzyme-catalyzed reactions. For example, it is a side-product of oxidases, resulting from the re-oxidation of FAD with molecular oxygen, and it is a substrate for peroxidases and other enzymes. However, hydrogen peroxide is able to chemically modify the peptide core of the enzymes it interacts with, and also to produce the oxidation of some cofactors and prostetic groups (e.g., the hemo group). Thus, the development of strategies that may permit to increase the stability of enzymes in the presence of this deleterious reagent is an interesting target. This enhancement in enzyme stability has been attempted following almost all available strategies: site-directed mutagenesis (eliminating the most reactive moieties), medium engineering (using stabilizers), immobilization and chemical modification (trying to generate hydrophobic environments surrounding the enzyme, to confer higher rigidity to the protein or to generate oxidation-resistant groups), or the use of systems capable of decomposing hydrogen peroxide under very mild conditions. If hydrogen peroxide is just a side-product, its immediate removal has been reported to be the best solution. In some cases, when hydrogen peroxide is the substrate and its decomposition is not a sensible solution, researchers coupled one enzyme generating hydrogen peroxide "in situ" to the target enzyme resulting in a continuous supply of this reagent at low concentrations thus preventing enzyme inactivation.This review will focus on the general role of hydrogen peroxide in biocatalysis, the main mechanisms of enzyme inactivation produced by this reactive and the different strategies used to prevent enzyme inactivation caused by this "dangerous liaison". Outlook

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Damage of amino acids and proteins induced by nitrogen dioxide, a free radical toxin, in air

Cited by 83 publications

References 33 publications

Effects of Oxygen on the Reactivity of Nitrogen Oxide Species Including Peroxynitrite

Effects of Oxygen on the Reactivity of Nitrogen Oxide Species Including Peroxynitrite

Free Radicals: Properties, Sources, Targets, and Their Implication in Various Diseases

Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

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