Internal electron transfer in Cu-heme oxidases: Thermodynamic or kinetic control (Articolo in rivista)

Type

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

Label

• Internal electron transfer in Cu-heme oxidases: Thermodynamic or kinetic control (Articolo in rivista) (literal)

Anno

• 1997-01-01T00:00:00+01:00 (literal)

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

• 10.1074/jbc.272.32.19870 (literal)

Alternative label

• Brunori M, Giuffrè A, D'Itri E, Sarti P (1997)
  Internal electron transfer in Cu-heme oxidases: Thermodynamic or kinetic control
  in The Journal of biological chemistry (Print)
  (literal)

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

• Brunori M, Giuffrè A, D'Itri E, Sarti P (literal)

Pagina inizio

• 19870 (literal)

Pagina fine

• 19874 (literal)

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

• cited By (since 1996)26 (literal)

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

• http://www.scopus.com/inward/record.url?eid=2-s2.0-0030752457&partnerID=40&md5=4a338b45354eabbc4da7601976ae45da (literal)

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

• 272 (literal)

Rivista

• ?The ?Journal of biological chemistry (Rivista)

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

• 32 (literal)

Note

• Scopu (literal)

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

• Dept. Biochem. Sci. A. Rossi-Fanelli, CNR Center of Molecular Biology, University of Rome La Sapienza, I-00185 Rome, Italy. (literal)

Titolo

• Internal electron transfer in Cu-heme oxidases: Thermodynamic or kinetic control (literal)

Abstract

• We present novel experimental evidence that, starting with the oxidized enzyme, the internal electron transfer in cytochrome c oxidase is kinetically controlled. The anaerobic reduction of the oxidized enzyme by ruthenium hexamine has been followed in the absence and presence of CO or NO, used as trapping ligands for reduced cytochrome a3. In the presence of NO, the rate of formation of the cytochrome a32+-NO adduct is independent of the concentration of ruthenium hexamine and of NO, indicating that in the oxidized enzyme cytochrome a and a3 are not in very rapid redox equilibrium; on the other hand, CO proved to be a poor 'trapping' ligand. We conclude that the intrinsic rate constant for a -> a3 electron transfer in the oxidized enzyme is 25 s-1. These data are discussed with reference to a model (Verkhovsky, M. I., Morgan, J. E., and Wikstrom, M. (1995) Biochemistry 34, 7483-7491) in which H+ diffusion and/or binding at the binuclear site is the rate-limiting step in the reduction of cytochrome a3 in the oxidized enzyme. (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

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

Insieme di parole chiave

• Keywords of "Internal electron transfer in Cu-heme oxidases: Thermodynamic or kinetic control" (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

• ?The ?Journal of biological chemistry (Rivista)

Insieme di parole chiave di

• Keywords of "Internal electron transfer in Cu-heme oxidases: Thermodynamic or kinetic control" (Insieme di parole chiave)