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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.

SUBMITTER: Faiella M

PROVIDER: S-EPMC3808167 | biostudies-literature | 2009 Dec

REPOSITORIES: biostudies-literature

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An artificial di-iron oxo-protein with phenol oxidase activity.

Faiella Marina M 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

Nature chemical biology 20091108 12

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. ...[more]

PMID: 19915535

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