Interaction of the bacterial terminal oxidase cytochrome bd with nitric oxide. (Articolo in rivista)

Type

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

Label

• Interaction of the bacterial terminal oxidase cytochrome bd with nitric oxide. (Articolo in rivista) (literal)

Anno

• 2004-01-01T00:00:00+01:00 (literal)

Alternative label

• Borisov VB; Forte E; Konstantinov AA; Poole RK; Sarti P; Giuffrè A. (2004)
  Interaction of the bacterial terminal oxidase cytochrome bd with nitric oxide.
  in FEBS letters (Print)
  (literal)

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

• Borisov VB; Forte E; Konstantinov AA; Poole RK; Sarti P; Giuffrè A. (literal)

Pagina inizio

• 201 (literal)

Pagina fine

• 204 (literal)

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

• 576 (literal)

Rivista

• FEBS letters (Rivista)

Note

• ISI Web of Science (WOS) (literal)

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

• A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Leninskie Gory, Moscow 119992, Russia; CNR Institute of Molecular Biology and Pathology, Department of Biochemical Sciences, University of Rome ''La Sapienza'', Rome I-00185, Italy; Department of Molecular Biology and Biotechnology, The University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, UK (literal)

Titolo

• Interaction of the bacterial terminal oxidase cytochrome bd with nitric oxide. (literal)

Abstract

• Cytochrome bd is a prokaryotic terminal oxidase catalyzing O2 reduction to H2O. The oxygen-reducing site has been proposed to contain two hemes, d and b595, the latter presumably replacing functionally CuB of heme-copper oxidases. We show that NO, in competition with O2, rapidly and potently (Ki =100+/-34 nM at ?70 uM O2) inhibits cytochrome bd isolated from Escherichia coli and Azotobacter vinelandii in turnover, inhibition being quickly and fully reverted upon NO depletion. Under anaerobic reducing conditions, neither of the two enzymes reveals NO reductase activity, which is proposed in heme-copper oxidases to be associated with CuB. (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' (Persona)

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' (Persona)

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

• FEBS letters (Rivista)