Aqueous Oxidation of Alcohols Catalyzed by Artificial Metalloenzymes Based on the Biotin–Avidin Technology
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.
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: ---