181655-43-6Relevant articles and documents
Chiral Zn-catalyzed aerobic oxidative kinetic resolution of α-hydroxy ketones
Muthupandi, Pandi,Sekar, Govindasamy
, p. 512 - 517 (2011)
The aerobic oxidative kinetic resolution of racemic α-hydroxy ketones was accomplished using a chiral Zn-quinine complex as the catalyst in the presence of molecular oxygen. The resulting optimized reaction conditions were applied to resolute different types of racemic α-hydroxy ketones and a maximum of 9.2 selectivity (s) was obtained with 88% ee for the recovered α-hydroxy ketone.
Base-Free Asymmetric Transfer Hydrogenation of 1,2-Di- and Monoketones Catalyzed by a (NH)2P2-Macrocyclic Iron(II) Hydride
De Luca, Lorena,Mezzetti, Antonio
supporting information, p. 11949 - 11953 (2017/09/20)
The hydride isonitrile complex [FeH(CNCEt3)(1 a)]BF4 (2) containing a chiral P2(NH)2 macrocycle (1 a), in the presence of 2-propanol as hydrogen donor, catalyzes the base-free asymmetric transfer hydrogenation (ATH) of prostereogenic ketones to alcohols and the hemihydrogenation of benzils to benzoins, which contain a base-labile stereocenter. Benzoins are formed in up to 83 % isolated yield with enantioselectivity reaching 95 % ee. Ketones give the same enantioselectivity observed with the parent catalytic system [Fe(CNCEt3)2(1 a)] (3 a) that operates with added NaOtBu.
Biocatalyzed asymmetric reduction of benzils to either benzoins or hydrobenzoins: pH dependent switch
Pal, Mohan,Srivastava, Gautam,Sharma, Amar Nath,Kaur, Suneet,Jolly, Ravinder S.
, p. 4017 - 4028 (2015/08/03)
Enantiopure benzoins and hydrobenzoins are precursors of various pharmaceuticals and biologically active compounds. In addition, hydrobenzoins are precursors of chiral ligands and auxiliaries in stereoselective organic synthesis. Biocatalytic reduction of benzils is a straightforward approach to prepare these molecules. However, known methods are not selective and lead to formation of a mixture of benzoin and hydrobenzoin, requiring expensive separation procedures. Here, we describe an enzyme system Talaromyces flavus, which exhibited excellent pH dependent selectivity for the conversion of benzil to either benzoin or hydrobenzion in high ee. Thus, (S)-benzoin was the exclusive product at pH 5.0 (ee >99%), whereas at pH 7.0, (S,S)-hydrobenzoin (ee >99%, dl/meso 97 : 3) was the exclusive product. The observed pH dependent selectivity was shown to be due to the presence of multiple enzymes in Talaromyces flavus, which specifically accepted either benzil or benzoin as a substrate and exhibited different pH profiles of their activity. The biocatalyst efficiently reduced a variety of symmetrical and unsymmetrical benzils. Moreover, a 36.4 kDa benzoin reductase was purified, the N-terminal sequence of which did not show a significant similarity to any of the known reductase/dehydrogenase in the database. The protein therefore appears to be a novel reductase.