A novel type of nitric-oxide reductase. Escherichia coli flavorubredoxin. (Articolo in rivista)

Type
Label
  • A novel type of nitric-oxide reductase. Escherichia coli flavorubredoxin. (Articolo in rivista) (literal)
Anno
  • 2002-01-01T00:00:00+01:00 (literal)
Alternative label
  • Gomes CM; Giuffrè A; Forte E; Vicente JB: Saraiva LM; Brunori M; Teixeira M. (2002)
    A novel type of nitric-oxide reductase. Escherichia coli flavorubredoxin.
    in The Journal of biological chemistry (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Gomes CM; Giuffrè A; Forte E; Vicente JB: Saraiva LM; Brunori M; Teixeira M. (literal)
Pagina inizio
  • 25273 (literal)
Pagina fine
  • 25276 (literal)
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  • This study is the result of a joint international project and was published in a high impact factor (IF = 6,696) scientific Journal for its potential implications in the bio-medicine field. This publication was cited 10 times. (literal)
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  • 277 (literal)
Rivista
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  • *Gomes CM and Giuffrè A contributed equally to the work (literal)
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  • This study provides original evidence for the existence of a novel enyzme family (the A-type flavoproteins) endowed with nitric oxide-reductase activity. These enzymes have been proposed to be involved in the defence response of pathogenic microorganisms to NO produced immunologically by the host upon infection. Testing such a hypothesis may provide the basis for novel pharmacology in the treatment of infectious diseases. (literal)
Note
  • ISI Web of Science (WOS) (literal)
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  • Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, APT 127, 2780-156 Oeiras, Portugal: Departamento de Quimica, Faculdade de Ciencias e Tecnologia, Universidade Nova de Lisboa, 2825-114 Caparica, Portugal;? Department of Biochemical Sciences and CNR Centre of Molecular Biology, University of Rome \"La Sapienza\", Rome 00185, Italy. (literal)
Titolo
  • A novel type of nitric-oxide reductase. Escherichia coli flavorubredoxin. (literal)
Abstract
  • Escherichia coli flavorubredoxin is a member of the family of the A-type flavoproteins, which are built by two core domains: a metallo-beta-lactamase-like domain, at the N-terminal region, harboring a non-heme di-iron site, and a flavodoxin-like domain, containing one FMN moiety. The enzyme from E. coli has an extra module at the C terminus, containing a rubredoxin-like center. The A-type flavoproteins are widespread among strict and facultative anaerobes, as deduced from the analysis of the complete prokaryotic genomes. In this report we showed that the recombinant enzyme purified from E. coli has nitric-oxide reductase activity with a turnover number of approximately 15 mol of NO.mol enzyme(-1).s(-1), which was well within the range of those determined for the canonical heme b(3)-Fe(B) containing nitric-oxide reductases (e.g. approximately 10-50 mol NO.mol enzyme(-1).s(-1) for the Paracoccus denitrificans NOR). Furthermore, it was shown that the activity was due to the A-type flavoprotein core, as the rubredoxin domain alone exhibited no activity. Thus, a novel family of prokaryotic NO reductases, with a non-heme di-iron site as the catalytic center, was established. (literal)
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