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.
Ligand type: Amino acidHost protein: Due Ferro 1Anchoring strategy: DativeOptimization: GeneticNotes: kcat/KM ≈ 1380 M-1*min-1
Artificial Heme Enzymes for the Construction of Gold-Based Biomaterials
Host protein: Mimochrome Fe(III)-S6G(D)-MC6 (De novo designed peptide)Anchoring strategy: CovalentOptimization: Chemical & geneticReaction: OxidationMax TON: ---ee: ---PDB: ---Notes: Immobilization of the ArM on gold surfaces via a lipoic acid anchor.