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