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Titolo:
Myoglobin-catalyzed tyrosine nitration: No need for peroxynitrite
Autore:
Kilinc, K; Kilinc, A; Wolf, RE; Grisham, MB;
Indirizzi:
Louisiana State Univ, Hlth Sci Ctr, Dept Cellular & Mol Physiol, Shreveport, LA 71130 USA Louisiana State Univ Shreveport LA USA 71130 ol, Shreveport, LA 71130 USA Louisiana State Univ, Hlth Sci Ctr, Dept Med, Shreveport, LA 71130 USA Louisiana State Univ Shreveport LA USA 71130 ed, Shreveport, LA 71130 USA
Titolo Testata:
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
fascicolo: 2, volume: 285, anno: 2001,
pagine: 273 - 276
SICI:
0006-291X(20010713)285:2<273:MTNNNF>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
NITRIC-OXIDE; HORSERADISH-PEROXIDASE; REPERFUSION INJURY; HYDROGEN-PEROXIDE; AUTOXIDATION; OXYMYOGLOBIN; SUPEROXIDE; MYELOPEROXIDASE; MECHANISM; NITROGEN;
Keywords:
hemoprotein; peroxidase; nitric oxide; ischemia; nitrotyrosine; reactive nitrogen species; hydrogen peroxide; inflammation; cardiovascular disease;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
32
Recensione:
Indirizzi per estratti:
Indirizzo: Grisham, MB Louisiana State Univ, Hlth Sci Ctr, Dept Cellular & Mol Physiol, POB 33932, Shreveport, LA 71130 USA Louisiana State Univ POB 33932 Shreveport LA USA 71130 130 USA
Citazione:
K. Kilinc et al., "Myoglobin-catalyzed tyrosine nitration: No need for peroxynitrite", BIOC BIOP R, 285(2), 2001, pp. 273-276

Abstract

The nitration of tyrosine residues in protein to yield 3-nitrotyrosine derivatives has been suggested to represent a specific footprint for peroxynitrite formation in vivo. However, recent studies suggest that certain hemoproteins such as peroxidases catalyze the H2O2-dependent nitration of tyrosine to yield 3-nitrotyrosine in a peroxynitrite-independent reaction. Because3-nitrotyrosine has been shown to be present in the postischemic myocardium, we wished to assess the ability of myoglobin to catalyze the nitration of tyrosine in vitro. We found that myoglobin catalyzed the oxidation of nitrite and promoted the nitration of tyrosine. Both nitrite oxidation and tyrosine nitration were H2O2-dependent and required the formation of ferryl (Fe+4) myoglobin. In addition, nitrite oxidation and tyrosine nitration were pH-dependent with a pH optimum of approximately 6.0. Taken together, these data suggest that the acidic pH and low oxygen tension produced during myocardial ischemia will facilitate myoglobin-catalyzed, peroxyntrite-independent formation of 3-nitrotyrosine, (C) 2001 Academic Press.

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Documento generato il 27/11/20 alle ore 21:40:23