An artificial di-iron oxo-protein with phenol oxidase activity (Articolo in rivista)

Type
Label
  • An artificial di-iron oxo-protein with phenol oxidase activity (Articolo in rivista) (literal)
Anno
  • 2009-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1038/nchembio.257 (literal)
Alternative label
  • Marina Faiella; Concetta Andreozzi; Rafael Torres Martin de Rosales; Vincenzo Pavone; Ornella Maglio; Flavia Nastri; William F. DeGrado; Angela Lombardi. (2009)
    An artificial di-iron oxo-protein with phenol oxidase activity
    in Nature chemical biology
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Marina Faiella; Concetta Andreozzi; Rafael Torres Martin de Rosales; Vincenzo Pavone; Ornella Maglio; Flavia Nastri; William F. DeGrado; Angela Lombardi. (literal)
Pagina inizio
  • 882 (literal)
Pagina fine
  • 884 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 5 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Department of Chemistry, University Federico II of Napoli, Napoli, Italy - Department of Biochemistry and Biophysics, University of Pennsylvania, School of Medicine, Philadelphia, Pennsylvania, USA - Division of Imaging Sciences, King's College London, St. Thomas Hospital, London, UK - Institute of Biostructure and Bioimaging, National Research Council (CNR), Napoli, Italy. (literal)
Titolo
  • An artificial di-iron oxo-protein with phenol oxidase activity (literal)
Abstract
  • Here we report the de novo design and NMR structure of a four-helical bundle di-iron protein with phenol oxidase activity. The introduction of the cofactor-binding and phenol binding sites required the incorporation of residues that were detrimental to the free energy of folding of the protein. Sufficient stability was, however, obtained by optimizing the sequence of a loop distant from the active site. (literal)
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Autore CNR

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