Dynamic kinetic resolution of allylic alcohols mediated by ruthenium- and lipase-based catalysts.
An enzyme-metal combo reaction has been developed for the dynamic kinetic resolution of allylic alcohols in which racemic substrates are transformed by a lipase and a ruthenium complex in the presence of an acyl donor to allylic acetates of high optical purity in over 80% yield.
Department of Chemistry, Division of Molecular and Life Science, Pohang University of Science and Technology, San 31 Hyojadong, Pohang, Kyungbuk 790-784, Korea.
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D
Lee
E A
EA
Huh
M J
MJ
Kim
H M
HM
Jung
J H
JH
Koh
J
J
Park
D002384:Catalysis; D004800:Enzymes, Immobilized / Q000378:metabolism; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D020005:Propanols / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism; D011549:Pseudomonas / Q000201:enzymology; D017975:Ruthenium Compounds / Q000378:metabolism*; D013237:Stereoisomerism
D004800:Enzymes, Immobilized; D020005:Propanols; D017975:Ruthenium Compounds; C006463:allyl alcohol; D008049:Lipase