title: An artificial di-iron oxo-protein with phenol oxidase activity.
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.
authors.affiliation: Department of Chemistry, University Federico II of Napoli, Complesso Universitario Monte S. Angelo, Italy.
authors.forename: Marina
authors.initials: M
authors.lastname: Faiella
authors.forename: Concetta
authors.initials: C
authors.lastname: Andreozzi
authors.forename: Rafael Torres Martin
authors.initials: RT
authors.lastname: de Rosales
authors.forename: Vincenzo
authors.initials: V
authors.lastname: Pavone
authors.forename: Ornella
authors.initials: O
authors.lastname: Maglio
authors.forename: Flavia
authors.initials: F
authors.lastname: Nastri
authors.forename: William F
authors.initials: WF
authors.lastname: DeGrado
authors.forename: Angela
authors.initials: A
authors.lastname: Lombardi
mesh_terms: D000595:Amino Acid Sequence; D002384:Catalysis; D020134:Catalytic Domain; D019295:Computational Biology; D033862:Iron-Binding Proteins / Q000737:chemistry* / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D014442:Monophenol Monooxygenase / Q000737:chemistry* / Q000235:genetics; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D015202:Protein Engineering; D013379:Substrate Specificity
chemical_list: D033862:Iron-Binding Proteins; D014442:Monophenol Monooxygenase