Investigating the mechanism of electron transfer to the binuclear center in Cu-heme oxidases (Articolo in rivista)

Type

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

Label

• Investigating the mechanism of electron transfer to the binuclear center in Cu-heme oxidases (Articolo in rivista) (literal)

Anno

• 1998-01-01T00:00:00+01:00 (literal)

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

• 10.1023/A:1020503410377 (literal)

Alternative label

• Brunori M, Giuffrè A, Malatesta F, Sarti P (1998)
  Investigating the mechanism of electron transfer to the binuclear center in Cu-heme oxidases
  in Journal of bioenergetics and biomembranes
  (literal)

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

• Brunori M, Giuffrè A, Malatesta F, Sarti P (literal)

Pagina inizio

• 41 (literal)

Pagina fine

• 45 (literal)

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

• cited By (since 1996)7 (literal)

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

• http://www.scopus.com/inward/record.url?eid=2-s2.0-7144255513&partnerID=40&md5=21281d7a3bcfda1d57faa75c5fd8bc1c (literal)

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

• 30 (literal)

Rivista

• Journal of bioenergetics and biomembranes (Rivista)

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

• 1 (literal)

Note

• Scopu (literal)

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

• Dept. Biochem. Sci. 'A Rossi-F.', CNR Center for Molecular Biology, University of Rome 'La Sapienza', I-00185 Rome, Italy; Department of Pure Biology, University of L'Aquila, I-6701 L'Aquila, Italy (literal)

Titolo

• Investigating the mechanism of electron transfer to the binuclear center in Cu-heme oxidases (literal)

Abstract

• Novel experimental evidence is presented further supporting the hypothesis that, starting with resting oxidized cytochrome c oxidase, the internal electron transfer to the oxygen binding site is kinetically controlled. The reduction of the enzyme was followed spectroscopically and in the presence of NO or CO, used as trapping ligands for reduced cytochrome a3; ruthenium hexamine was used as a spectroscopically silent electron donor. Consistent with the high combination rate constant for reduced cytochrome a3, NO proved to be a very efficient trapping ligand, while CO did not. The results are discussed in view of two alternative (thermodynamic and kinetic) hypotheses of control of electron transfer to the binuclear (cyt.a3-Cu(B)) center. Fulfilling the prediction of the kinetic control hypothesis: i) the reduction of cytochrome a3 and ligation are synchronous and proceed at the intrinsic rate of cytochrome a3 reduction, ii) the measured rate of formation of the nitrosyl derivative is independent of the concentration of both the reductant and NO. (literal)

Prodotto di

• 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

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

Insieme di parole chiave

• Parole chiave di "Investigating the mechanism of electron transfer to the binuclear center in Cu-heme oxidases" (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

• Journal of bioenergetics and biomembranes (Rivista)

Insieme di parole chiave di

• Parole chiave di "Investigating the mechanism of electron transfer to the binuclear center in Cu-heme oxidases" (Insieme di parole chiave)