Spectroscopic and metal-binding properties of DF3: an artificial protein able to accommodate different metal ions (Articolo in rivista)

Type
Label
  • Spectroscopic and metal-binding properties of DF3: an artificial protein able to accommodate different metal ions (Articolo in rivista) (literal)
Anno
  • 2010-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1007/s00775-010-0639-9 (literal)
Alternative label
  • Martin de Rosales Rafael Torres; Faiella Marina; Farquhar Erik; Que Lawrence Jr.; Andreozzi Concetta; Pavone Vincenzo; Maglio Ornella; Nastri Flavia; Lombardi Angela (2010)
    Spectroscopic and metal-binding properties of DF3: an artificial protein able to accommodate different metal ions
    in JBIC. Journal of biological inorganic chemistry (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Martin de Rosales Rafael Torres; Faiella Marina; Farquhar Erik; Que Lawrence Jr.; Andreozzi Concetta; Pavone Vincenzo; Maglio Ornella; Nastri Flavia; Lombardi Angela (literal)
Pagina inizio
  • 717 (literal)
Pagina fine
  • 728 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 15 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Department of Chemistry, University of Naples ''Federico II'', Napoli - Department of Chemistry,Centre for Metals in Biocatalysis, University of Minnesota, Minneapolis - IBB, CNR, Naples. (literal)
Titolo
  • Spectroscopic and metal-binding properties of DF3: an artificial protein able to accommodate different metal ions (literal)
Abstract
  • The design, synthesis, and metal-binding properties of DF3, a new de novo designed di-iron protein model are described (''DF'' represents due ferri, Italian for ''two iron,'' ''di-iron''). DF3 is the latest member of the DF family of synthetic proteins. They consist of helix-loop-helix hairpins, designed to dimerize and form an antiparallel four-helix bundle that encompasses a metal-binding site similar to those of non-heme carboxylate-bridged di-iron proteins. Unlike previous DF proteins, DF3 is highly soluble in water (up to 3 mM) and forms stable complexes with several metal ions (Zn, Co, and Mn), with the desired secondary structure and the expected stoichiometry of two ions per protein. UV-vis studies of Co(II) and Fe(III) complexes confirm a metal-binding environment similar to previous di- Co(II)- and di-Fe(III)-DF proteins, including the presence of a l-oxo-di-Fe(III) unit. Interestingly, UV-vis, EPR, and resonance Raman studies suggest the interaction of a tyrosine adjacent to the di-Fe(III) center. The design of DF3 was aimed at increasing the accessibility of small molecules to the active site of the four-helix bundle. Indeed, binding of azide to the di-Fe(III) site demonstrates a more accessible metal site compared with previous DFs. In fact, fitting of the binding curve to the Hill equation allows us to quantify a 150% accessibility enhancement, with respect to DF2. All these results represent a significant step towards the development of a functional synthetic DF metalloprotein. (literal)
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