http://www.cnr.it/ontology/cnr/individuo/prodotto/ID174939
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)
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- 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)
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