New Aspects in the Reaction Mechanism of Phenol with Peroxynitrite: The Role of Phenoxy Radicals

Daiber, Andreas; Mehl, Martin; Ullrich, Volker

doi:10.1006/niox.1998.0186

Cited by 61 publications

(54 citation statements)

References 41 publications

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“…Tyrosine Nitration in Proteins-The mechanisms of tyrosine nitration studied with just free tyrosine dissolved in simple phosphate buffers have been used to make deductions about how tyrosine is nitrated in proteins in vivo (32,50,60). In simple solutions, radical processes can certainly be the major cause of nitration and dimerization by peroxynitrite.…”

Section: Discussionmentioning

confidence: 99%

Superoxide Reacts with Nitric Oxide to Nitrate Tyrosine at Physiological pH via Peroxynitrite

Reiter

Teng

Beckman

2000

Journal of Biological Chemistry

368

238

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Tyrosine nitration is a widely used marker of peroxynitrite (ONOO ؊ ) produced from the reaction of nitric oxide with superoxide. Pfeiffer and Mayer (Pfeiffer, S., and Mayer, B. (1998) J. Biol. Chem. 273, 27280 -27285) reported that superoxide produced from hypoxanthine plus xanthine oxidase in combination with nitric oxide produced from spermine NONOate did not nitrate tyrosine at neutral pH. They suggested that nitric oxide and superoxide at neutral pH form a less reactive intermediate distinct from preformed alkaline peroxynitrite that does not nitrate tyrosine. Using a stopped-flow spectrophotometer to rapidly mix potassium superoxide with nitric oxide at pH 7.4, we report that an intermediate spectrally and kinetically identical to preformed alkaline cis-peroxynitrite was formed in 100% yield. Furthermore, this intermediate nitrated tyrosine in the same yield and at the same rate as preformed peroxynitrite. Equivalent concentrations of nitric oxide under aerobic conditions in the absence of superoxide did not produce detectable concentrations of nitrotyrosine. Carbon dioxide increased the efficiency of nitration by nitric oxide plus superoxide to the same extent as peroxynitrite. In experiments using xanthine oxidase as a source of superoxide, tyrosine nitration was substantially inhibited by urate formed from hypoxanthine oxidation, which was sufficient to account for the lack of tyrosine nitration previously reported. We conclude that peroxynitrite formed from the reaction of nitric oxide with superoxide at physiological pH remains an important species responsible for tyrosine nitration in vivo.

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Section: Discussionmentioning

confidence: 99%

Superoxide Reacts with Nitric Oxide to Nitrate Tyrosine at Physiological pH via Peroxynitrite

Reiter

Teng

Beckman

2000

Journal of Biological Chemistry

368

238

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“…An electron transfer mechanism has also been proposed to explain the peroxynitrite (or nitrosoperoxycarbonate)-mediated oxidation of phenolic compounds (Pryor & Squadrito, 1995;Daiber, Mehl, & Ullrich, 1998). In both these mechanisms (radical or electron transfer), the intermediacy of a phenoxyl radical has been proposed (Pryor & Squadrito, 1995;Butler et al, 1997;Daiber, Mehl, & Ullrich, 1998), and more recently demonstrated (Grossi, 2003). Regardless of the step that leads to the formation of a Tyr radical (or phenoxyl radical), the total product (3-nitrotyrosine plus dityrosine) will essentially depend of the concentration of the Tyr radical (Fig.…”

Section: Posttranslational Modification Of Proteinsmentioning

confidence: 99%

Current analytical methods for the detection of dityrosine, a biomarker of oxidative stress, in biological samples

DiMarco

Giulivi

2006

Mass Spectrometry Reviews

121

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Dityrosine is a fluorescent molecule formed as a result of normal posttranslational processing. In many structural proteins, dityrosine confers resistance to proteolysis and physicochemical trauma as a stabilizing crosslink. Dityrosine has also been found in oxidative/nitrative stress under a variety of conditions and biological systems. In this regard, it has been used as an important biomarker for oxidatively modified proteins during UV and gamma-irradiation, aging, and exposure to oxygen free radicals, nitrogen dioxide, peroxynitrite, and lipid hydroperoxides. Renewed interest in dityrosine and other tyrosine oxidation products as clinical indicators of oxidative modification has driven the development of important techniques for the specific analysis and quantification of these molecules. The presence of elevated levels of dityrosine in mammalian tissue and urine samples has been measured by chromatographic separation followed by mass spectrometry GC-MS and HPLC-MS/MS. Increases in dityrosine levels have been associated with pathologies such as eye cataracts, atherosclerosis, acute inflammation, and Alzheimer's disease. The continued development of, and increased accessibility to, improved mass spectrometric instrumentation will expand the capability, feasibility, and sensitivity with which specific biomarkers like dityrosine can be measured.

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“…Compound 2, dissolved in H 2 O in the presense of phenol, leads to nitrated and hydroxylated products; benzene-1,4-diol (hydroquinone), benzene-1,2-diol (catechol), 4-nitrophenol, and 2-nitrophenol were identified by HPLC [10]. Three additional, unidentified peaks were assigned to phenol dimers [11].…”

Section: Ooh]mentioning

confidence: 99%

“…The acid is a powerful oxidant [5] that damages biological compounds [6 ± 9]. Aside from one-electron and two-electron oxidations, it reacts with phenolic compounds to form nitrated, hydroxylated, and dimerized products [10] [11]. Indeed, the nitration of free tyrosine, or tyrosine in proteins, has served as a marker of peroxynitrite formation in vivo [12].…”

mentioning

confidence: 99%

Synthesis and Characterization of Tris(tetraethylammonium) Pentacyanoperoxynitritocobaltate(III)

Wick¹,

Kissner²,

Koppenol³

2000

HCA

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New Aspects in the Reaction Mechanism of Phenol with Peroxynitrite: The Role of Phenoxy Radicals

Cited by 61 publications

References 41 publications

Superoxide Reacts with Nitric Oxide to Nitrate Tyrosine at Physiological pH via Peroxynitrite

Superoxide Reacts with Nitric Oxide to Nitrate Tyrosine at Physiological pH via Peroxynitrite

Current analytical methods for the detection of dityrosine, a biomarker of oxidative stress, in biological samples

Synthesis and Characterization of Tris(tetraethylammonium) Pentacyanoperoxynitritocobaltate(III)

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