1072879-63-0Relevant articles and documents
-
Ren, Hong,Mukherjee, Munmun,Wulff, William D.,Desai, Aman A.
, p. 1108 - 1115 (2011)
-
BOROX catalysis: Self-assembled AMINO-BOROX and IMINO-BOROX chiral Bronsted acids in a five component catalyst assembly/ catalytic asymmetric aziridination
Gupta, Anil K.,Mukherjee, Munmun,Hu, Gang,Wulff, William D.
supporting information, p. 7932 - 7944,13 (2020/10/15)
A five-component catalyst assembly/aziridination reaction is described starting from an aldehyde, an amine, ethyl diazoacetate, B(OPh)3, and a molecule of a vaulted biaryl ligand (VAPOL or VANOL). A remarkable level of chemoselectivity was observed since, while 10 different products could have resulted from various reactions between the five components, an aziridine was formed in 85% yield and 98% ee and only two other products could be detected in 3% yield. Studies reveal that the first in a sequence of three reactions is an exceedingly rapid amine-induced assembly of an AMINOBOROX chiral Bronsted acid species from VAPOL and B(OPh)3, which is followed by imine formation from the amine and aldehyde and the concomitant formation of an IMINO-BOROX chiral Bronsted acid and finally the reaction of the imine with ethyl diazoacetate mediated by the IMINO-BOROX catalyst to give aziridine-2-carboxylic esters with very high diastereo- and enantioselectivity.
Substrate-induced covalent assembly of a chemzyme and crystallographic characterization of a chemzyme-substrate complex
Hu, Gang,Gupta, Anil K.,Huang, Rui H.,Mukherjee, Munmun,Wulff, William D.
supporting information; experimental part, p. 14669 - 14675 (2010/12/25)
A substrate induced covalent assembly of a highly organized chemzyme known to be effective in both catalytic asymmetric aziridination and aza Diels-Alder reactions is described and the information gained from which led to an efficient one-pot aziridination protocol. The crystal structures of two chemzyme-iminium complexes were elucidated by X-ray diffraction analysis that provides critical insights into the binding of the substrates with the chemzyme.