29076-84-4Relevant articles and documents
Hydrogen bond directed aerobic oxidation of amines via photoredox catalysis
Wang, Hongyu,Man, Yunquan,Wang, Kaiye,Wan, Xiuyan,Tong, Lili,Li, Na,Tang, Bo
supporting information, p. 10989 - 10992 (2018/10/08)
An application of H-bonding interactions for directing the α-C-H oxidation of amines to amides and amino-ketones catalyzed by an organic photocatalyst is reported. The high efficiency of this method is demonstrated by the aerobic oxidation of pyrrolidines, diarylamines and benzylamines bearing urea groups with high yields and a wide substrate scope.
Organocatalytic Enantioselective Synthesis of Tetrahydrofluoren-9-ones via Vinylogous Michael Addition/Henry Reaction Cascade of 1,3-Indandione-Derived Pronucleophiles
M?hlmann, Lennart,Chang, Geng-Hua,Madhusudhan Reddy,Lee, Chia-Jui,Lin, Wenwei
supporting information, p. 688 - 691 (2016/03/01)
An unprecedented organocatalytic enantioselective vinylogous Michael addition/Henry cyclization cascade is presented for the synthesis of highly substituted tetrahydrofluoren-9-ones 3 employing novel 1,3-indandione-derived pronucleophiles 1a-g and nitroalkenes 2. Following a very simple protocol, a wide range of products were obtained in good to excellent yields and with excellent enantioinduction (43-98% yield, up to 98% ee). The reaction proceeded with excellent diastereocontrol despite the simultaneous generation of four stereogenic centers. Surprisingly, when 2-(1-phenylethylidene)-1H-indandione (1h) was used as a pronucleophile, no cyclization was observed, and only Michael addition adducts 4a-x were furnished in very good yields and excellent enantioselectivities. (Chemical Equation Presented).
Tailoring D-amino acid oxidase from the pig kidney to r-stereoselective amine oxidase and its use in the deracemization of α-methylbenzylamine
Yasukawa, Kazuyuki,Nakano, Shogo,Asano, Yasuhisa
, p. 4428 - 4431 (2014/05/06)
The deracemization of racemic amines to yield enantioenriched amines using S-stereoselective amine oxidases (AOx) has recently been attracting attention. However, R-stereoselective AOx that are suitable for deracemization have not yet been identified. An R-stereoselective AOx was now evolved from porcine kidney D-amino acid oxidase (pkDAO) and subsequently use for the deracemization of racemic amines. The engineered pkDAO, which was obtained by directed evolution, displayed a markedly changed substrate specificity towards R?amines. The mutant enzyme exhibited a high preference towards the substrate α- methylbenzylamine and was used to synthesize the S?amine through deracemization. The findings of this study indicate that further investigations on the structure-activity relationship of AOx are warranted and also provide a new method for biotransformations in organic synthesis. A change in selectivity: An engineered porcine kidney D-amino acid oxidase (pkDAO) with markedly changed substrate selectivity towards R?amines was obtained by directed evolution. The mutant enzyme exhibited a high preference towards the substrate α-methylbenzylamine and was used to synthesize the S-configured amine through deracemization.