Interaction of nitric oxide with the activity of cytosolic NADH/cytochrome c electron transport system (Articolo in rivista)

Type
Label
  • Interaction of nitric oxide with the activity of cytosolic NADH/cytochrome c electron transport system (Articolo in rivista) (literal)
Anno
  • 2009-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.abb.2009.07.020 (literal)
Alternative label
  • Marzulli, Domenico; Gorgoglione, Vincenza ; Palmitessa, Valeria; La Piana, Gianluigi; Lofrumento, Nicola Elio; Laraspata, Daniela (2009)
    Interaction of nitric oxide with the activity of cytosolic NADH/cytochrome c electron transport system
    in Archives of biochemistry and biophysics (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Marzulli, Domenico; Gorgoglione, Vincenza ; Palmitessa, Valeria; La Piana, Gianluigi; Lofrumento, Nicola Elio; Laraspata, Daniela (literal)
Pagina inizio
  • 99 (literal)
Pagina fine
  • 109 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 489 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 10 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 1-2 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Department of Biochemistry and Molecular Biology, University of Bari Institute of Biomembranes and Bioenergetics (literal)
Titolo
  • Interaction of nitric oxide with the activity of cytosolic NADH/cytochrome c electron transport system (literal)
Abstract
  • Nitric oxide ({radical dot}NO) generated by the dissociation of S-nitrosoglutathione or added as gaseous solution, inhibits the oxidation of exogenous NADH supported by the activity of the cytosolic NADH/cyto-c electron transport pathway. The inhibition is immediate, very strong, higher at lower oxygen concentration, independent on the {radical dot}NO concentration and remains constant as long as {radical dot}NO is no more available and then is spontaneously removed. The data obtained, not in contrast with those reported with isolated cytochrome oxidase (Cox), strengthen a new concept: reduced cytochrome c (cyto-c) and {radical dot}NO behave as two substrates of Cox, which promotes their oxidation with molecular oxygen as a co-substrate. In the presence of {radical dot}NO, Cox exhibits the property of switching from cyto-c oxidase to {radical dot}NO oxidase activity. With an \"all or nothing\" process Cox becomes an efficient {radical dot}NO scavenger. The persistence of membrane potential, even in the presence of high inhibition of oxygen uptake, could be tentatively correlated to the protective effect of {radical dot}NO on the ischaemic-reperfusion injury (literal)
Prodotto di
Autore CNR
Insieme di parole chiave

Incoming links:


Prodotto
Autore CNR di
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
Insieme di parole chiave di
data.CNR.it