Enantioselective oxidation of secondary alcohols by the flavoprotein alcohol oxidase from Phanerochaete chrysosporium

The enantioselective oxidation of secondary alcohols represents a valuable approach for the synthesis optically pure compounds. Flavoprotein oxidases can catalyse such selective transformations by merely using oxygen as electron acceptor. While many flavoprotein preferably act on primary alcohols, FAD-containing alcohol oxidase from Phanerochaete chrysosporium was found to be able perform kinetic resolutions several alcohols. By (S)-alcohols, (R)-alcohols were obtained in high enantiopurity. In silico docking studies carried out order substantiate observed (S)-selectivity. Several hydrophobic and aromatic residues substrate binding site create cavity which substrates comfortably undergo van der Waals pi-stacking interactions. Consequently, is restricted one two enantiomers. This study has uncovered ability an oxidase, that known oxidizing small oxidations various