Available information on the molecular mechanisms by which nitric oxide (NO) controls the activity of the respiratory enzyme (cytochrome-c-oxidase) is reviewed. We report that, depending on absolute electron flux, NO at physiological concentrations reversibly inhibits cytochrome-c-oxidase by two alternative reaction pathways, yielding either a nitrosyl- or a nitrite-heme a(3) derivative. We address a number of hypotheses, envisaging physiological and/or pathological effects of the reactions between NO and cytochrome-c-oxidase. (c) 2006 Elsevier B.V. All rights reserved.
Nitric oxide and the respiratory enzyme / Brunori, Maurizio; Forte, Elena; Arese, Marzia; Mastronicola, Daniela; Giuffre', Alessandro; Sarti, Paolo. - In: BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS. - ISSN 0005-2728. - 1757:9-10(2006), pp. 1144-1154. (Intervento presentato al convegno Bari Conference on Mitochondria and Bioenergetics tenutosi a Bari, ITALY nel DEC, 2005) [10.1016/j.bbabio.2006.05.011].
Nitric oxide and the respiratory enzyme
BRUNORI, Maurizio;FORTE, Elena;ARESE, Marzia;MASTRONICOLA, Daniela;GIUFFRE', ALESSANDRO;SARTI, Paolo
2006
Abstract
Available information on the molecular mechanisms by which nitric oxide (NO) controls the activity of the respiratory enzyme (cytochrome-c-oxidase) is reviewed. We report that, depending on absolute electron flux, NO at physiological concentrations reversibly inhibits cytochrome-c-oxidase by two alternative reaction pathways, yielding either a nitrosyl- or a nitrite-heme a(3) derivative. We address a number of hypotheses, envisaging physiological and/or pathological effects of the reactions between NO and cytochrome-c-oxidase. (c) 2006 Elsevier B.V. All rights reserved.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.