Litcius/Paper detail

Production of Hydroxy Acids: Selective Double Oxidation of Diols by Flavoprotein Alcohol Oxidase

Caterina Martin, Miloš Trajković, Marco W. Fraaije

2020Angewandte Chemie International Edition44 citationsDOIOpen Access PDF

Abstract

Flavoprotein oxidases can catalyze oxidations of alcohols and amines by merely using molecular oxygen as the oxidant, making this class of enzymes appealing for biocatalysis. The FAD-containing (FAD=flavin adenine dinucleotide) alcohol oxidase from P. chrysosporium facilitated double and triple oxidations for a range of aliphatic diols. Interestingly, depending on the diol substrate, these reactions result in formation of either lactones or hydroxy acids. For example, diethylene glycol could be selectively and fully converted into 2-(2-hydroxyethoxy)acetic acid. Such a facile cofactor-independent biocatalytic route towards hydroxy acids opens up new avenues for the preparation of polyester building blocks.

Topics & Concepts

FlavoproteinChemistryOxidase testAlcoholOrganic chemistryBiochemistryEnzymeEnzyme Catalysis and ImmobilizationMetal-Catalyzed Oxygenation MechanismsOxidative Organic Chemistry Reactions
Production of Hydroxy Acids: Selective Double Oxidation of Diols by Flavoprotein Alcohol Oxidase | Litcius