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;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.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/365237
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