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Elsevier, Tetrahedron: Asymmetry, 8(22), p. 916-923

DOI: 10.1016/j.tetasy.2011.05.009

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

Journal article published in 2011 by Jürgen Brem ORCID, Sarolta Pilbák, Csaba Paizs, Gergely Bánóczi, Florin-Dan Irimie, Monica-Ioana Toşa, László Poppe
This paper was not found in any repository, but could be made available legally by the author.
This paper was not found in any repository, but could be made available legally by the author.

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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 rac2a–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.