This paper reports 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.
An artificial di-iron oxo-protein with phenol oxidase activity / Faiella, Marina; C., Andreozzi; R., Torres; Pavone, Vincenzo; O., Maglio; Nastri, Flavia; W. F., Degrado; Lombardi, Angelina. - In: NATURE CHEMICAL BIOLOGY. - ISSN 1552-4450. - STAMPA. - 5:12(2009), pp. 882-884. [10.1038/nchembio.257]
An artificial di-iron oxo-protein with phenol oxidase activity
FAIELLA, MARINA;PAVONE, VINCENZO;NASTRI, FLAVIA;LOMBARDI, ANGELINA
2009
Abstract
This paper reports 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.File | Dimensione | Formato | |
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