An artificial di-iron oxo-protein with phenol oxidase activity.
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.
Faiella
Marina
M
Department of Chemistry, University Federico II of Napoli, Complesso Universitario Monte S. Angelo, Italy.
Andreozzi
Concetta
C
de Rosales
Rafael Torres Martin
RT
Pavone
Vincenzo
V
Maglio
Ornella
O
Nastri
Flavia
F
DeGrado
William F
WF
Lombardi
Angela
A
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
D033862:Iron-Binding Proteins; D014442:Monophenol Monooxygenase