Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
70781 | Journal of Molecular Catalysis B: Enzymatic | 2009 | 5 Pages |
Abstract
An alcohol dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus (PFADH) effectively catalyzed the reductions of various substituted α-chloroacetophenones to furnish the corresponding (R)-configurated α-chlorohydrins with excellent enantiomeric purity. The co-factor NADH could be recycled with d-glucose dehydrogenase/d-glucose system or in a coupled substrate approach using iso-propanol as the hydrogen donor. The hydrogen transfer mode should be more cost-effective. Thus, the PFADH-catalyzed hydrogen transfer reductions of some substrates were carried out on the preparative scale, demonstrating that this enzyme would be a valuable biocatalyst for the preparation of chiral chlorohydrins of pharmaceutical interest.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Catalysis
Authors
Dunming Zhu, Brooke A. Hyatt, Ling Hua,