Catalytic Promiscuity of Galactose Oxidase: A Mild Synthesis of Nitriles from Alcohols, Air, and Ammonia. Issue 43 (8th October 2018)

• Record Type: Journal Article
• Authors: Vilím, Jan; Knaus, Tanja; Mutti, Francesco G.
• Is Part Of: Angewandte Chemie international edition. Volume 57:Issue 43(2018)
• Page Start: 14240
• Page End: 14244
• Publication Date: 2018-10-08
• Subjects: alcohol oxidation -- biocatalysis -- catalytic promiscuity -- copper oxidases -- nitriles; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201809411
• Languages: English
• ISSNs: 1433-7851

Abstract

Abstract: We report an unprecedented catalytically promiscuous activity of the copper‐dependent enzyme galactose oxidase. The enzyme catalyses the one‐pot conversion of alcohols into the related nitriles under mild reaction conditions in ammonium buffer, consuming ammonia as the source of nitrogen and dioxygen (from air at atmospheric pressure) as the only oxidant. Thus, this green method does not require either cyanide salts, toxic metals, or undesired oxidants in stoichiometric amounts. The substrate scope of the reaction includes benzyl and cinnamyl alcohols as well as 4‐ and 3‐pyridylmethanol, giving access to valuable chemical compounds. The oxidation proceeds through oxidation from alcohol to aldehyde, in situ imine formation, and final direct oxidation to nitrile. Abstract : Unprecedented catalytic promiscuity of a copper‐dependent alcohol oxidase enables the one‐pot transformation of selected alcohols into nitriles under mild, cyanide‐free conditions using ammonia as the nitrogen donor and dioxygen as the oxidant. This reaction provides a valuable addition to enzymatic methods for nitrile synthesis, since direct enzymatic transformation of alcohols into nitriles has so far been unknown.