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Nat Chem Biol. 2009 Dec;5(12):882-4. doi: 10.1038/nchembio.257. Epub 2009 Nov 8.

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

Author information

1
Department of Chemistry, University Federico II of Napoli, Complesso Universitario Monte S. Angelo, Italy.

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.

PMID:
19915535
PMCID:
PMC3808167
DOI:
10.1038/nchembio.257
[Indexed for MEDLINE]
Free PMC Article

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