188839-74-9Relevant articles and documents
Reductive Coupling of Aromatic Aldehydes and Ketones under Electrochemical Conditions
Li, Qian-Yu,Swaroop, Toreshettahally R.,Wang, Heng Shan,Wang, Zi-Qiang
, (2020/04/27)
Reductive coupling of o-substituted carbonyl compounds and m-substituted carbonyl compounds by the direct transfer of electron to carbonyl group respectively gave 1-(4-(1-hydroxy-1-phenylethyl/methyl)phenyl)ethanones/methanones and 2,3-bis(3-substitutedph
Stereoselective Barbier-Type Allylations and Propargylations Mediated by CpTiCl3
López-Martínez, Josefa L.,Torres-García, Irene,Rodríguez-García, Ignacio,Mu?oz-Dorado, Manuel,álvarez-Corral, Miriam
, p. 806 - 816 (2019/01/24)
CpTiCl2, prepared in situ by manganese reduction of CpTiCl3, is an excellent new system for the Barbier-type allylation and propargylation of carbonyl compounds. It can be used in catalytic amounts when combined with Et3N·HBr/TMSBr, which acts as a regenerating system. The high regio- and stereoselectivity shown by this system makes it useful for prenylation and crotylation processes in the synthesis of natural products.
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.