Conversion of alcohols to enantiopure amines through dual enzyme hydrogen-borrowing cascades

Mutti, F.G.*; Knaus, T.; Scrutton, N.S.; Breuer, M.; Turner, N. J.*;

Science, 2015, 349 (6255), 1525-1529. DOI: 10.1126/science.aac9283 (open access: http://europepmc.org/articles/PMC4883652)

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A biocatalytic hydrogen-borrowing amination of primary and secondary alcohols that allows for the efficient and environmentally benign production of enantiopure amines is presented. The method relies on a combination of two enzymes: an alcohol dehydrogenase operating in tandem with an amine dehydrogenase to aminate a structurally diverse range of aromatic and aliphatic alcohols, yielding up to 96% conversion and 99% enantiomeric excess. Primary alcohols were aminated with high conversion (up to 99%). This redox self-sufficient network possesses high atom efficiency, sourcing nitrogen from ammonium and generating water as the sole by-product.

 
 
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