The cytochrome cbb3 from Pseudomonas stutzeri displays nitric oxide reductase activity (Articolo in rivista)

Type

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

Label

• The cytochrome cbb3 from Pseudomonas stutzeri displays nitric oxide reductase activity (Articolo in rivista) (literal)

Anno

• 2001-01-01T00:00:00+01:00 (literal)

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

• 10.1046/j.0014-2956.2001.02597.x (literal)

Alternative label

• Forte E, Urbani A, Saraste M, Sarti P, Brunori M, Giuffrè A (2001)
  The cytochrome cbb3 from Pseudomonas stutzeri displays nitric oxide reductase activity
  in European journal of biochemistry (Print)
  (literal)

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

• Forte E, Urbani A, Saraste M, Sarti P, Brunori M, Giuffrè A (literal)

Pagina inizio

• 6486 (literal)

Pagina fine

• 6490 (literal)

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

• cited By (since 1996)62 (literal)

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

• http://www.scopus.com/inward/record.url?eid=2-s2.0-0035543035&partnerID=40&md5=8cc9958d1b542fc5fe14505380954b40 (literal)

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

• 268 (literal)

Rivista

• European journal of biochemistry (Rivista)

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

• 24 (literal)

Note

• Scopu (literal)

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

• Department of Biochemical Sciences, CNR Centre of Molecular Biology, University of Rome 'La Sapienza', Rome, Italy; European Molecular Biology Laboratory, Heidelberg, Germany. (literal)

Titolo

• The cytochrome cbb3 from Pseudomonas stutzeri displays nitric oxide reductase activity (literal)

Abstract

• The cytochrome cbb3 is an isoenzyme in the family of cytochrome c oxidases. This protein purified from Pseudomonas stutzeri displays a cyanide-sensitive nitric oxide reductase activity (Vmax = 100 ± 9 mol NO·mol cbb3 -1·min-1 and Km = 12 ± 2.5 ?M), which is lost upon denaturation. This enzyme is only partially reduced by ascorbate, and readily re-oxidized by NO under anaerobic conditions at a rate consistent with the turnover number for NO consumption. As shown by transient spectroscopy experiments and singular value decomposition (SVD) analysis, these results suggest that the cbb3-type cytochromes, sharing structural features with bacterial nitric oxide reductases, are the enzymes retaining the highest NO reductase activity within the heme-copper oxidase superfamily. (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

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

Insieme di parole chiave

• Keywords of "The cytochrome cbb3 from Pseudomonas stutzeri displays nitric oxide reductase activity" (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

• European journal of biochemistry (Rivista)

Insieme di parole chiave di

• Keywords of "The cytochrome cbb3 from Pseudomonas stutzeri displays nitric oxide reductase activity" (Insieme di parole chiave)