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Titolo:
Cytochrome c nitration by peroxynitrite
Autore:
Cassina, AM; Hodara, R; Souza, JM; Thomson, L; Castro, L; Ischiropoulos, H; Freeman, BA; Radi, R;
Indirizzi:
Univ Republ, Fac Med, Dept Bioquim, Montevideo 11800, Uruguay Univ RepublMontevideo Uruguay 11800 Bioquim, Montevideo 11800, Uruguay Univ Republ, Fac Ciencias, Inst Quim Biol, Lab Enzimol, Montevideo 11800, Uruguay Univ Republ Montevideo Uruguay 11800 Enzimol, Montevideo 11800, Uruguay Childrens Hosp Philadelphia, Dept Pediat, Philadelphia, PA 19104 USA Childrens Hosp Philadelphia Philadelphia PA USA 19104 lphia, PA 19104 USA Univ Alabama, Dept Anesthesiol, Birmingham, AL 35233 USA Univ Alabama Birmingham AL USA 35233 nesthesiol, Birmingham, AL 35233 USA Univ Alabama, Dept Biochem, Birmingham, AL 35233 USA Univ Alabama Birmingham AL USA 35233 pt Biochem, Birmingham, AL 35233 USA Univ Alabama, Dept Mol Genet, Birmingham, AL 35233 USA Univ Alabama Birmingham AL USA 35233 Mol Genet, Birmingham, AL 35233 USA Univ Alabama, UAB Ctr Rad Biol, Birmingham, AL 35233 USA Univ Alabama Birmingham AL USA 35233 r Rad Biol, Birmingham, AL 35233 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 28, volume: 275, anno: 2000,
pagine: 21409 - 21415
SICI:
0021-9258(20000714)275:28<21409:CCNBP>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
MITOCHONDRIAL ELECTRON-TRANSPORT; MANGANESE-SUPEROXIDE-DISMUTASE; NITRIC-OXIDE SYNTHASE; TYROSINE NITRATION; HYDROGEN-PEROXIDE; HORSERADISH-PEROXIDASE; REVERSIBLE INHIBITION; CATALYZED OXIDATION; LIPID-PEROXIDATION; RESPIRATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
59
Recensione:
Indirizzi per estratti:
Indirizzo: Radi, R Univ Republ, Fac Med, Dept Bioquim, Ave Gen Flores 2125, Montevideo 11800,Uruguay Univ Republ Ave Gen Flores 2125 Montevideo Uruguay 11800 ,Uruguay
Citazione:
A.M. Cassina et al., "Cytochrome c nitration by peroxynitrite", J BIOL CHEM, 275(28), 2000, pp. 21409-21415

Abstract

Peroxynitrite (ONOO-), the product of superoxide (O-2(.-)) and nitric oxide ((NO)-N-.) reaction, inhibits mitochondrial respiration and can stimulateapoptosis. Cytochrome c, a mediator of these two aspects of mitochondrial function, thus represents an important potential target of ONOO- during conditions involving accelerated rates of oxygen radical and (NO)-N-. generation. Horse heart cytochrome c(3+) was nitrated by ONOO-, as indicated by spectral changes, Western blot analysis, and mass spectrometry. A dose-dependent loss of cytochrome c(3+) 695 nm absorption occurred, inferring that nitration of a critical heme-vicinal tyrosine (Tyr-67) promoted a conformational change, displacing the Met-80 heme ligand. Nitration was confirmed by cross-reactivity with a specific antibody against 3-nitrotyrosine and by increased molecular mass compatible with the addition of a nitro-(-NO2) group. Mass analysis of tryptic digests indicated the preferential nitration of Tyr-67 among the four conserved tyrosine residues in cytochrome c. Cytochrome c(3+) was more extensively nitrated than cytochrome c(2+) because of the preferential oxidation of the reduced heme by ONOO-. Similar protein nitration patterns were obtained by ONOO- reaction in the presence of carbon dioxide, whereupon secondary nitrating species arise from the decomposition of the nitroso-peroxocarboxylate (ONOOCO2-) intermediate. Peroxynitrite-nitratedcytochrome c displayed significant changes in redox properties, including (a) increased peroxidatic activity, (b) resistance to reduction by ascorbate, and (c) impaired support of state 4-dependent respiration in intact rat heart mitochondria. These results indicate that cytochrome c nitration may represent both oxidative and signaling events occurring during (NO)-N-.- and ONOO--mediated cell injury.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 20:17:06