Lipase-catalyzed kinetic resolutions of racemic 1-(10-ethyl-10H- phenothiazin-1,2, and 4-yl)ethanols and their acetates

Jürgen Brem, Sarolta Pilbák, Csaba Paizs, Gergely Bánóczi, Florin Dan Irimie, Monica Ioana Toşa, László Poppe

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

The synthesis of both enantiomers of 1-(10-ethyl-10H-phenothiazin-1,2, and 4-yl)ethanols 1a-c and their acetates via enantioselective methanolysis of the corresponding racemic esters rac 2a-c with lipase B from Candida antarctica (CaL-B) or/and by acylation of the racemic alcohols with the lipase A or lipase B from C. antarctica (CaL-A and CaL-B) is described. The absolute configuration of enantiopure 1-(10-ethyl-10H-phenothiazin-1-yl)ethyl acetate 2a was assigned as (R) by using QM/MM(hf/3-21g:uff) calculations within the CaL-B (1LBT crystal structure) enzymic environment.

Original languageEnglish
Pages (from-to)916-923
Number of pages8
JournalTetrahedron Asymmetry
Volume22
Issue number8
DOIs
Publication statusPublished - Apr 30 2011

ASJC Scopus subject areas

  • Catalysis
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry

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