Enzyme-Catalyzed Nucleophilic Ring Opening of Epoxides for the Preparation of Enantiopure Tertiary Alcohols

Maja Majeric Elenkov, H. Wolfgang Hoeffken, Lixia Tang, Bernhard Hauer, Dick B. Janssen

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Abstract

The halohydrin dehalogenase from Agrobacterium radiobacter AD1 (HheC) catalyzes nucleophilic ring opening of epoxides with cyanide and azide. In the case of 2,2-disubstituted epoxides, this reaction proceeds with excellent enantioselectivity (E values up to >200), which gives, by kinetic resolution, access to various enantiopure epoxides and β-substituted tertiary alcohols (ee up to 99%). Since the enzyme has a broad substrate range and because these tertiary alcohols are difficult to prepare in other ways, HheC is an attractive biocatalyst for the production of β-cyano and β-azido tertiary alcohols.
Original languageEnglish
Number of pages7
JournalChemInform
Volume39
Issue number7
Publication statusPublished - 2007

Keywords

  • tertiary alcohols
  • kinetic resolution
  • dehalogenase
  • halohydrin
  • epoxides
  • cyanides
  • azides

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