An Artificial Di-Iron Oxo-Orotein with Phenol Oxidase Activity
Nat. Chem. Biol. 2009, 5, 882-884, 10.1038/nchembio.257
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.
Max TON: >50ee: ---PDB: 2KIKNotes: kcat/KM ≈ 1380 M-1*min-1
Reaction: Amine oxidationMax TON: ---ee: ---PDB: 2KIKNotes: kcat/KM ≈ 83 M-1*min-1
Aqueous Oxidation of Alcohols Catalyzed by Artificial Metalloenzymes Based on the Biotin–Avidin Technology
J. Organomet. Chem. 2005, 690, 4488-4491, 10.1016/j.jorganchem.2005.02.001
Based on the incorporation of biotinylated organometallic catalyst precursors within (strept)avidin, we have developed artificial metalloenzymes for the oxidation of secondary alcohols using tert-butylhydroperoxide as oxidizing agent. In the presence of avidin as host protein, the biotinylated aminosulfonamide ruthenium piano stool complex 1 (0.4 mol%) catalyzes the oxidation of sec-phenethyl alcohol at room temperature within 90 h in over 90% yield. Gel electrophoretic analysis of the reaction mixture suggests that the host protein is not oxidatively degraded during catalysis.
Ligand type: Amino-sulfonamide; BenzeneMax TON: 200ee: ---PDB: ---Notes: ---
Ligand type: Amino-sulfonamide; BenzeneHost protein: Avidin (Av)Max TON: 230ee: ---PDB: ---Notes: ---
Ligand type: Bipyridine; C6Me6Max TON: 173ee: ---PDB: ---Notes: ---
Metal: RhLigand type: Amino-sulfonamide; Cp*Max TON: 7.5ee: ---PDB: ---Notes: ---
Metal: IrLigand type: Bipyridine; Cp*Max TON: 30ee: ---PDB: ---Notes: ---
De Novo Design of Catalytic Proteins
Proc. Natl. Acad. Sci. U. S. A. 2004, 101, 11566-11570, 10.1073/pnas.0404387101
The de novo design of catalytic proteins provides a stringent test of our understanding of enzyme function, while simultaneously laying the groundwork for the design of novel catalysts. Here we describe the design of an O2-dependent phenol oxidase whose structure, sequence, and activity are designed from first principles. The protein catalyzes the two-electron oxidation of 4-aminophenol (k cat/K M = 1,500 M·1·min·1) to the corresponding quinone monoimine by using a diiron cofactor. The catalytic efficiency is sensitive to changes of the size of a methyl group in the protein, illustrating the specificity of the design.
Max TON: >100ee: ---PDB: ---Notes: kcat/KM ≈ 1540 M-1*min-1