You are currently viewing the abstract.
View Full TextLog in to view the full text
AAAS login provides access to Science for AAAS members, and access to other journals in the Science family to users who have purchased individual subscriptions.
Register for free to read this article
As a service to the community, this article is available for free. Existing users log in.
More options
Download and print this article for your personal scholarly, research, and educational use.
Buy a single issue of Science for just $15 USD.
A clean and green approach to amines
Enzymes evolved to operate in water and to modify their substrates using comparatively nontoxic reagents. Thus, a major advantage of applying enzymes to synthetic chemistry is their compatibility with environmentally benign conditions. Mutti et al. report that two enzymes—alcohol and amine dehydrogenases—can operate in tandem to convert alcohols to amines. The reaction proceeds with ammonium as the only input and water as the only byproduct. The mechanism relies on consecutive oxidation and reduction steps, with hydrogen shuttled by a nicotinamide coenzyme.
Science, this issue p. 1525
Abstract
α-Chiral amines are key intermediates for the synthesis of a plethora of chemical compounds at industrial scale. We present a biocatalytic hydrogen-borrowing amination of primary and secondary alcohols that allows for the efficient and environmentally benign production of enantiopure amines. The method relies on a combination of two enzymes: an alcohol dehydrogenase (from Aromatoleum sp., Lactobacillus sp., or Bacillus sp.) operating in tandem with an amine dehydrogenase (engineered from Bacillus sp.) 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 cascade possesses high atom efficiency, sourcing nitrogen from ammonium and generating water as the sole by-product.
