Redox properties of the oxygen-detoxifying flavodiiron protein from the human parasite Giardia intestinalis (Articolo in rivista)

Type
Label
  • Redox properties of the oxygen-detoxifying flavodiiron protein from the human parasite Giardia intestinalis (Articolo in rivista) (literal)
Anno
  • 2009-01-01T00:00:00+01:00 (literal)
Alternative label
  • Vicente JB; Testa F; Mastronicola D;, Forte E;, Sarti P; Teixeira M; Giuffrè A. (2009)
    Redox properties of the oxygen-detoxifying flavodiiron protein from the human parasite Giardia intestinalis
    in Archives of biochemistry and biophysics (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Vicente JB; Testa F; Mastronicola D;, Forte E;, Sarti P; Teixeira M; Giuffrè A. (literal)
Pagina inizio
  • 9 (literal)
Pagina fine
  • 13 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 488 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Instituto de Tecnologia Quimica e Biologica, Universidade Nova de Lisboa, Av. da Republica (EAN), 2781-901 Oeiras, Portugal; Department of Biochemical Sciences, CNR Institute of Molecular Biology and Pathology, and Istituto Pasteur-Fondazione Cenci Bolognetti, Sapienza University of Rome, Rome I-00185, Italy. (literal)
Titolo
  • Redox properties of the oxygen-detoxifying flavodiiron protein from the human parasite Giardia intestinalis (literal)
Abstract
  • Flavodiiron proteins (FDPs) are enzymes identified in prokaryotes and a few pathogenic protozoa, which protect microorganisms by reducing O2 to H2O and/or NO to N2O. Unlike most prokaryotic FDPs, the protozoan enzymes from the human pathogens Giardia intestinalis and Trichomonas vaginalis are selective towards O2. UV/vis and EPR spectroscopy showed that, differently from the NO-consuming bacterial FDPs, the Giardia FDP contains an FMN with reduction potentials for the formation of the single and the two-electron reduced forms very close to each other (E1 = ?66 ± 15 mV and E2 = ?83 ± 15 mV), a condition favoring destabilization of the semiquinone radical. Giardia FDP contains also a non-heme diiron site with significantly up-shifted reduction potentials (E1 = +163 ± 20 mV and E2 = +2 ± 20 mV). These properties are common to the Trichomonas hydrogenosomal FDP, and likely reflect yet undetermined subtle structural differences in the protozoan FDPs, accounting for their marked O2 specificity. (literal)
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