1314850-97-9Relevant articles and documents
RETRACTED ARTICLE: Site-selective enzymatic C-H amidation for synthesis of diverse lactams
Cho, Inha,Jia, Zhi-Jun,Arnold, Frances H.
, p. 575 - 578 (2019)
A major challenge in carbon?hydrogen (C?H) bond functionalization is to have the catalyst control precisely where a reaction takes place. In this study, we report engineered cytochrome P450 enzymes that perform unprecedented enantioselective C?H amidation reactions and control the site selectivity to divergently construct b-, g-, and d-lactams, completely overruling the inherent reactivities of the C?H bonds. The enzymes, expressed in Escherichia coli cells, accomplish this abiological carbon?nitrogen bond formation via reactive iron-bound carbonyl nitrenes generated from nature-inspired acyl-protected hydroxamate precursors. This transformation is exceptionally efficient (up to 1,020,000 total turnovers) and selective (up to 25:1 regioselectivity and 97%, please refer to compound 2v enantiomeric excess), and can be performed easily on preparative scale.
Synthesis of γ-, δ-, and ε-lactams by asymmetric transfer hydrogenation of N-(tert-butylsulfinyl)iminoesters
Guijarro, David,Pablo, Oscar,Yus, Miguel
, p. 3647 - 3654 (2013/05/22)
Highly enantiomerically enriched γ- and δ-lactams have been prepared by a simple and very efficient procedure that involves the asymmetric transfer hydrogenation of N-(tert-butylsulfinyl)iminoesters followed by desulfinylation of the nitrogen atom and spo
