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Titolo:
Reaction mechanism between nitric oxide and glutathione mediated by Fe(III) myoglobin
Autore:
Reichenbach, G; Sabatini, S; Palombari, R; Palmerini, CA;
Indirizzi:
Univ Perugia, Dipartimento Chim, Perugia, Italy Univ Perugia Perugia Italy v Perugia, Dipartimento Chim, Perugia, Italy Univ Perugia, Dipartimento Biol Cellulare & Mol, Perugia, Italy Univ Perugia Perugia Italy timento Biol Cellulare & Mol, Perugia, Italy
Titolo Testata:
NITRIC OXIDE-BIOLOGY AND CHEMISTRY
fascicolo: 4, volume: 5, anno: 2001,
pagine: 395 - 401
SICI:
1089-8603(200108)5:4<395:RMBNOA>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
GUANYLATE-CYCLASE; S-NITROSOTHIOLS; SERUM-ALBUMIN; BLOOD; HEME; NO; FERRIHEMOPROTEINS; PHOTOLYSIS; ACTIVATION; PRESSURE;
Keywords:
myoglobin; nitric oxide; nitrosoglutathione; reaction mechanism;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
32
Recensione:
Indirizzi per estratti:
Indirizzo: Reichenbach, G Univ Perugia, Dipartimento Chim, Via Elce Sotto 8, Perugia,Italy Univ Perugia Via Elce Sotto 8 Perugia Italy erugia, Italy
Citazione:
G. Reichenbach et al., "Reaction mechanism between nitric oxide and glutathione mediated by Fe(III) myoglobin", NITRIC OXID, 5(4), 2001, pp. 395-401

Abstract

Ferrimyoglobin at pH 7.4 binds nitric oxide to yield nitric oxide adducts. In the presence of glutathione (GSH), nitrosoadducts of Mb(III) react withit to give nitrosoglutathione, whose concentration has been determined with an apparatus based on a specific and sensitive solid-state amperometric gas sensor. The reaction constant between the adduct and glutathione, k(GSH)= (47 +/-1) M-1 s(-1), obtained by UV-Vis spectroscopy kinetic measurements, is about one-eighth of the constant with OH- determined by other authors. We can explain this fact with the higher nucleophilicity of OH- compared to GSH, due to the bulkiness and charge of the species. It is known that the formation of nitrosothiols starting from nitrite or NO (nitrogen monoxide) and glutathione, in the absence of oxygen, is impossible. Thus, from a biological point of view, it is important to point out that GSH reacts with NO in the presence of ferrimyoglobin, even at physiological pH, to form nitrosoglutathione. (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 10/04/20 alle ore 14:37:15