Kinetics of superoxide dismutase- and iron-catalyzed nitration of phenolics by peroxynitrite

Beckman, Joseph S.; Ischiropoulos, Harry; Zhu, Ling; Woerd, Mark van der; Smith, Craig D.; Chen, Jun; Harrison, Joseph G.; Martin, J. C.; Tsai, Michael Y.

doi:10.1016/0003-9861(92)90432-v

Cited by 747 publications

(427 citation statements)

References 23 publications

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“…Nitration of tyrosine and phenolics by peroxynitrite has been reported to be catalyzed by ferric ion [4,25]. We have examined the effects of ferric and ferrous ion on nitroSGua formation in DNA.…”

Section: Resultsmentioning

confidence: 99%

Formation of 8‐nitroguanine in DNA treated with peroxynitrite in vitro and its rapid removal from DNA by depurination

1995

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Peroxynitrite is a strong oxidant formed by reaction of nitric oxide with superoxide in inflamed tissues. We have demonstrated that 8-nitroguanine is formed dose-dependently in calf thymus DNA incubated with low concentrations of peroxynitrite in vitro. 8-Nitroguanine in acid-hydrolyzed DNA was chemically reduced into 8-aminoguanine, which was analyzed using high performance liquid chromatography with electrochemical detection. Only peroxynitrite, but not nitrite, tetranitromethane nor NO-releasing compounds, formed 8-nitroguanine. Antioxidants and desferrioxamine inhibited the reaction. 8-Nitroguanine was depurinated from DNA incubated at pH 7.4, 37°C (tu2 = -4 h). Peroxynitrite did not increase 8-oxoguanine levels in DNA.

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Section: Resultsmentioning

confidence: 99%

Formation of 8‐nitroguanine in DNA treated with peroxynitrite in vitro and its rapid removal from DNA by depurination

1995

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“…The catalysis was not directly related to plasma NO concentrations, peroxynitrite availability, or secondary alternations associated with the SOD1 knockout. More than a decade after the demonstration of SOD1 in catalyzing nitrotyrosine formation in vitro [9,10,14], we have provided direct evidence for such a role of SOD1 in vivo. The application of mass spectrometry and proteomic analysis helps elucidate the structural mechanism for that catalytic function of SOD1 and the metabolic implications.…”

mentioning

confidence: 85%

Role of copper,zinc-superoxide dismutase in catalyzing nitrotyrosine formation in murine liver

Zhu

Zhang

Roneker

et al. 2008

Free Radical Biology and Medicine

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The solely known function of Cu,Zn-superoxide dismutase (SOD1) is to catalyze the dismutation of superoxide anion into hydrogen peroxide. Our objective was to determine if SOD1 catalyzed murine liver protein nitration induced by acetaminophen (APAP) and lipopolysaccharide (LPS). Liver and plasma samples were collected from young adult SOD1 knockout mice (SOD1-/-) and wild-type (WT) mice at 5 or 6 h after an ip injection of saline, APAP, or LPS. Hepatic nitrotyrosine formation was induced by APAP and LPS only in the WT mice. The diminished hepatic protein nitration in the SOD1-/-mice was not directly related to plasma nitrite and nitrate concentrations. Similar genotype differences were seen in liver homogenates treated with a bolus of peroxynitrite. Adding only the holo, but not the apo-SOD1 enzyme into the liver homogenates enhanced the reaction in an activity-dependent fashion and nearly eliminated the genotype difference at the high doses. Mass Spectrometry showed 4 more nitrotyrosine residues in bovine serum albumin and 10 more nitrated protein candidates in the SOD1-/-liver homogenates by peroxynitrite with added SOD1. In conclusion, the diminished hepatic protein nitration mediated by APAP or LPS in the SOD1-/-mice was due to the lack of SOD1 activity per se. Keywords SOD1; Protein nitration; Acetaminophen; Peroxynitrite; Lipopolysaccharide; Mouse Although copper,zinc-superoxide dismutase (SOD1) has been widely considered a major intracellular antioxidant enzyme in mammals, its solely known function is to catalyze the conversion of superoxide anion into less active hydrogen peroxide. Indeed, SOD1 is protective against oxidative stress associated with acute paraquat toxicity, myocardial ischemia/reperfusion injury, and N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced dopaminergic neurodegeneration [1][2][3]. Mice deficient in SOD1 develop Address correspondence to: Xin Gen Lei, Department of Animal Science, Cornell University, Ithaca, NY 14853, Tel. 607-254-4703; Fax. 607-255-9829; E-Mail: XL20@cornell.edu. Publisher's Disclaimer: This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final citable form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. [7,8]. These paradoxical findings strongly suggest that SOD1 may exert functions more than just superoxide dismutation. In fact, SOD1 was shown to promote peroxynitrite-mediated nitrotyrosine formation in vitro [9,10]. NIH Public AccessPeroxynitrite is formed by a rapid diffusion-limited, radical-radical coupling reaction between nitric oxide (NO) and superoxide anion [11,12] [24,25,33,34] provide us with an unprecedented opportunity to study the in vivo role of SOD1 in nitrotyrosine formation. Furtherm...

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“…Unlike (pK 4.8), PN (with a pK of 6.8) can easily penetrate cells in the protonated form because of its high diffusibility across phospholipid membranes (Marla et al, 1997). PN is known to initiate oxidative modification of proteins, including the nitration of aromatic rings (Beckman et al, 1992), sulfoxidation of methionin, and S-nitrosation of cysteine followed by disulfide formation, thereby rendering inactive certain functionally important regulatory proteins, like receptors or enzymes (Haddad et al, 1994). Nitration of tyrosine is the underlying mechanism of prostacyclin synthase inhibition by PN (Zou et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

Superoxide as a Messenger of Endothelial Function

Ullrich

Bachschmid²

2000

Biochemical and Biophysical Research Communications

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Kinetics of superoxide dismutase- and iron-catalyzed nitration of phenolics by peroxynitrite

Cited by 747 publications

References 23 publications

Formation of 8‐nitroguanine in DNA treated with peroxynitrite in vitro and its rapid removal from DNA by depurination

Formation of 8‐nitroguanine in DNA treated with peroxynitrite in vitro and its rapid removal from DNA by depurination

Role of copper,zinc-superoxide dismutase in catalyzing nitrotyrosine formation in murine liver

Superoxide as a Messenger of Endothelial Function

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