37778-99-7Relevant articles and documents
Chelation and Stereodirecting Group Effects on Regio- And Diastereoselective Samarium(II)-Water Allylic Benzoate Reductions
Leitch, Michael A.,O'Neil, Gregory W.,Stockdale, Trevor F.
, p. 1544 - 1560 (2020)
SmI 2 (H 2 O) n reductions of allylic benzoates adjacent to a trisubstituted alkene occur in high yields with complete regioselectivity and good diastereoselectivity (up to 90:10) for substrates containing properly positioned stereodirecting- and chelating groups. The outcome of these reactions can be rationalized by ring conformation considerations of a proposed chelated organosamarium intermediate, and a mechanism involving intramolecular protonation by a samarium-bound water.
Structural Elucidation of the Mechanism of Molecular Recognition in Chiral Crystalline Sponges
Fairen-Jimenez, David,Zaworotko, Michael J.,Zhang, Shi-Yuan
supporting information, p. 17600 - 17606 (2020/08/12)
To gain insight into chiral recognition in porous materials we have prepared a family of fourth generation chiral metal–organic frameworks (MOFs) that have rigid frameworks and adaptable (flexible) pores. The previously reported parent material, [Co2(S-mandelate)2(4,4′-bipyridine)3](NO3)2, CMOM-1S, is a modular MOF; five new variants in which counterions (BF4?, CMOM-2S) or mandelate ligands are substituted (2-Cl, CMOM-11R; 3-Cl, CMOM-21R; 4-Cl, CMOM-31R; 4-CH3, CMOM-41R) and the existing CF3SO3? variant CMOM-3S are studied herein. Fine-tuning of pore size, shape, and chemistry afforded a series of distinct host–guest binding sites with variable chiral separation properties with respect to three structural isomers of phenylpropanol. Structural analysis of the resulting crystalline sponge phases revealed that host–guest interactions, guest–guest interactions, and pore adaptability collectively determine chiral discrimination.
Identification of an Esterase Isolated Using Metagenomic Technology which Displays an Unusual Substrate Scope and its Characterisation as an Enantioselective Biocatalyst
Gavin, Declan P.,Murphy, Edel J.,Foley, Aoife M.,Castilla, Ignacio Abreu,Reen, F. Jerry,Woods, David F.,Collins, Stuart G.,O'Gara, Fergal,Maguire, Anita R.
, p. 2466 - 2474 (2019/03/11)
Evaluation of an esterase annotated as 26D isolated from a marine metagenomic library is described. Esterase 26D was found to have a unique substrate scope, including synthetic transformations which could not be readily effected in a synthetically useful manner using commercially available enzymes. Esterase 26D was more selective towards substrates which had larger, more sterically demanding substituents (i. e. iso-propyl or tert-butyl groups) on the β-carbon, which is in contrast to previously tested commercially available enzymes which displayed a preference for substrates with sterically less demanding substituents (e.g. methyl group) at the β-carbon. (Figure presented.).
