Journal
CATALYSIS SCIENCE & TECHNOLOGY
Volume 10, Issue 7, Pages 2145-2151Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/d0cy00081g
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Funding
- National Natural Science Foundation of China [31571775]
- Key Laboratory of Environmental and Applied Microbiology of the Chinese Academy of Sciences [KLCAS-2018-1]
- Major Science and Technology Projects in Henan Province [192102110163]
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Asymmetric epoxidation is a green route to enantiopure epoxides, but often suffers from low enantioselectivity toward unconjugated terminal alkenes. Mining of the NCBI non-redundant protein sequences with a reconstructed ancestral sequence based on six styrene monooxygenases identified a monooxygenase (HhMo) from Herbaspirillum huttiense with 29.6-32.3% sequence identity with styrene monooxygenases, which was previously annotated as an alanine phosphoribitol ligase. HhMo catalyzed the epoxidation of allylbenzenes with moderate to excellent enantioselectivity yielding the corresponding epoxides in up to 99% ee. The HhMo-catalyzed epoxidation could also achieve the kinetic resolution of racemic secondary allylic alcohols, yielding the corresponding epoxides with up to 50% yields, as well as excellent enantio- and diastereoselectivity (up to >99% ee and >99% de) within 20-60 min, making a greener strategy for the production of valuable enantiopure glycidol derivatives in the fine chemical and pharmaceutical industries.
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