257941-62-1Relevant articles and documents
Access to Wieland-Miescher ketone in an enantiomerically pure form by a kinetic resolution with yeast-mediated reduction
Fuhshuku, Ken-Ichi,Funa, Nobutaka,Akeboshi, Tomohiro,Ohta, Hiromichi,Hosomi, Hiroyuki,Ohba, Shigeru,Sugai, Takeshi
, p. 129 - 135 (2000)
Both enantiomers of Wieland-Miescher ketone [3,4,8,8a-tetrahydro-8a- methyl-1,6(2H, 7H)-naphthalenedione], in a highly enantiomerically enriched form, became readily available by a newly developed kinetic resolution with yeast-mediated reduction. From a screening of yeast strains, Torulaspora delbrueckii IFO 10921 was selected. The collected cells of this strain, obtained by an incubation in a glucose medium, smoothly reduced only the isolated carbonyl group of the (S)enantiomer, while the (R)-enantiomer remained intact. Starting from both enantiomers (~70% ee) prepared by an established proline-mediated asymmetric Robinson annulation, the reduction with T. delbrueckii gave the (R)-enantiomer (98% ee) and the corresponding alcohol (4aS,5S)-4,4a,5,6,7,8-hexahydro-5-hydroxy-4a-methyl-2(3H)- naphthalenone (94% ee, 94% de) in preparative scale in nearly quantitative yields. An approach for the asymmetric synthesis of the Wieland-Miescher ketone was also successful. 2-Methyl-2-(3-oxobutyl)-1,3-cyclohexanedione, the prochiral precursor, was reduced with this strain to give a cyclic acetal form of (2S,3S)-3-hydroxy-2-methyl-2-(3-oxobutyl)cyclohexanone, in a stereomerically pure form.
Enzymatic Baeyer-Villiger oxidation of bicyclic diketones
Ottolina, Gianluca,De Gonzalo, Gonzalo,Carrea, Giacomo,Danieli, Bruno
, p. 1035 - 1040 (2007/10/03)
Cyclohexanone monooxygenase from Acinetobacter calcoaceticus was employed for the Baeyer-Villiger oxidation of racemic bicyclic diketones such as the Wieland-Miescher and the Hajos-Parrish diketones and of some of their derivatives. The corresponding lactones were produced in a highly regio-and enantioselective manner. The reactions were carried out using a crude enzyme preparation in aqueous buffer, at room temperature, and the recycling of the expensive coenzyme NADPH was conducted with a second ancillary enzymatic system. The enzymatic process was simple and easy to handle, thus providing a very practical tool to access enantiopure lactones.
