| Literature DB >> 16792997 |
Maurizio Brunori1, Elena Forte, Marzia Arese, Daniela Mastronicola, Alessandro Giuffrè, Paolo Sarti.
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 a3 derivative. We address a number of hypotheses, envisaging physiological and/or pathological effects of the reactions between NO and cytochrome-c-oxidase.Entities:
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Year: 2006 PMID： 16792997 DOI： 10.1016/j.bbabio.2006.05.011
Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002