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.
Notes: kcat/KM ≈ 1380 M-1*min-1
Aqueous Oxidation of Alcohols Catalyzed by Artificial Metalloenzymes Based on the Biotin–Avidin Technology
Max TON: 200ee: ---PDB: ---Notes: ---
Host protein: Avidin (Av)Max TON: 230ee: ---PDB: ---Notes: ---
Max TON: 173ee: ---PDB: ---Notes: ---
Metal: RhMax TON: 7.5ee: ---PDB: ---Notes: ---