Nitric oxide, cytochrome c oxidase and myoglobin: competition and reaction pathways. (Articolo in rivista)

Type
Label
  • Nitric oxide, cytochrome c oxidase and myoglobin: competition and reaction pathways. (Articolo in rivista) (literal)
Anno
  • 2005-01-01T00:00:00+01:00 (literal)
Alternative label
  • Giuffrè A; Forte E; Brunori M; Sarti P. (2005)
    Nitric oxide, cytochrome c oxidase and myoglobin: competition and reaction pathways.
    in FEBS letters (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Giuffrè A; Forte E; Brunori M; Sarti P. (literal)
Pagina inizio
  • 2528 (literal)
Pagina fine
  • 2532 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 579 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Department of Biochemical Sciences and CNR Institute of Molecular Biology and Pathology, University of Rome ''La Sapienza'', I-00185 Rome, Italy. (literal)
Titolo
  • Nitric oxide, cytochrome c oxidase and myoglobin: competition and reaction pathways. (literal)
Abstract
  • It is relevant to cell physiology that nitric oxide (NO) reacts with both cytochrome oxidase (CcOX) and oxygenated myoglobin (MbO2). In this respect, it has been proposed [Pearce, L.L., et al. (2002) J. Biol. Chem. 277, 13556-13562] that (i) CcOX in turnover out-competes MbO2 for NO, and (ii) NO bound to reduced CcOX is ''metabolized'' in the active site to nitrite by reacting with O2. In contrast, rapid kinetics experiments reported in this study show that (i) upon mixing NO with MbO2 and CcOX in turnover, MbO2 out-competes the oxidase for NO and (ii) after mixing nitrosylated CcOX with O2 in the presence of MbO2, NO (and not nitrite) dissociates from the enzyme causing myoglobin oxidation. (literal)
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