Nitric oxide and cytochrome c oxidase: Mechanisms of inhibition and NO degradation (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• Nitric oxide and cytochrome c oxidase: Mechanisms of inhibition and NO degradation (Articolo in rivista) (literal)

Anno

• 2000-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1006/bbrc.2000.3117 (literal)

Alternative label

• Sarti P, Giuffrè A, Forte E, Mastronicola D, Barone MC, Brunori M (2000)
  Nitric oxide and cytochrome c oxidase: Mechanisms of inhibition and NO degradation
  in Biochemical and biophysical research communications (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Sarti P, Giuffrè A, Forte E, Mastronicola D, Barone MC, Brunori M (literal)

Pagina inizio

• 183 (literal)

Pagina fine

• 187 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#altreInformazioni

• cited By (since 1996)92 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url

• http://www.scopus.com/inward/record.url?eid=2-s2.0-0033941097&partnerID=40&md5=aff884848b0a77a366429c1ffcde4c6c (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 274 (literal)

Rivista

• Biochemical and biophysical research communications (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

• 1 (literal)

Note

• Scopu (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Department of Biochemical Sciences, CNR Center of Molecular Biology, University of Rome la Sapienza, Rome, Italy (literal)

Titolo

• Nitric oxide and cytochrome c oxidase: Mechanisms of inhibition and NO degradation (literal)

Abstract

• NO inhibits mitochondrial respiration by reacting with either the reduced or the oxidized binuclear site of cytochrome c oxidase, leading respectively to accumulation of cytochrome a32+-NO or cytochrome a33+-NO2- species. Exploiting the unique light sensitivity of the cytochrome a32+-NO, we show that under turnover conditions, depending on the cytochrome c2+ concentration, either the cytochrome a32+-NO or the nitrite-bound enzyme is formed. The predominance of one of the two inhibitory pathways depends on the occupancy of the turnover intermediates. In the dark, the respiration recovers at the rate of NO dissociation (k' = 0.01 s-1 at 37°C). Illumination of the sample speeds up recovery rate only at higher reductant concentrations, indicating that the inhibited species is cytochrome a32+-NO. When the reaction occurs with the oxidized binuclear site, light has no effect and NO is oxidized to harmless nitrite eventually released in the bulk, accounting for catalytic NO degradation. (C) 2000 Academic Press. (literal)

Prodotto di

• Biologia strutturale e bioinformatica: struttura-funzione, dinamica e riconoscimento in proteine (SV.P14.008.001) (Modulo)
• Institute of molecular biology and pathology (IBPM) (Istituto)

Autore CNR

• MAURIZIO BRUNORI (Persona)
• ALESSANDRO GIUFFRE' (Unità di personale interno)

Insieme di parole chiave

• Parole chiave di "Nitric oxide and cytochrome c oxidase: Mechanisms of inhibition and NO degradation" (Insieme di parole chiave)

Incoming links:

Prodotto

• Institute of molecular biology and pathology (IBPM) (Istituto)
• Biologia strutturale e bioinformatica: struttura-funzione, dinamica e riconoscimento in proteine (SV.P14.008.001) (Modulo)

Autore CNR di

• ALESSANDRO GIUFFRE' (Unità di personale interno)
• MAURIZIO BRUNORI (Persona)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Biochemical and biophysical research communications (Rivista)

Insieme di parole chiave di

• Parole chiave di "Nitric oxide and cytochrome c oxidase: Mechanisms of inhibition and NO degradation" (Insieme di parole chiave)