An Artificial Di-Iron Oxo-Orotein with Phenol Oxidase Activity
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.
kcat/KM ≈ 1380 M-1*min-1