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From Theozymes to Artificial Enzymes: Enzyme‐Like Receptors for Michael Additions with Oxyanion Holes and Active Amino Groups (Eur. J. Org. Chem. 29/2007)
Author(s) -
Simón Luis,
Muñiz Francisco M.,
Sáez Silvia,
Raposo César,
Morán Joaquín R.
Publication year - 2007
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/ejoc.200790076
Subject(s) - chemistry , oxyanion hole , oxyanion , catalysis , enzyme , stereochemistry , michael reaction , amine gas treating , enzyme catalysis , active site , catalytic triad , receptor , combinatorial chemistry , organic chemistry , biochemistry
The cover picture shows the design of molecular receptors with enzyme‐like catalytic activity for the Michael addition of pyrrolidine to an α,β‐unsaturated lactam. The picture emphasizes the design process of these receptors by using a draft‐like style for the receptor structure. This design is based on a model for the transition state (represented as a high‐quality 3‐D model) that is obtained from theoretical study of the reaction mechanism. In the paper, we use both kinetic experiments and molecular modeling studies to assist the design of the H‐bonding catalyst. From these studies we concluded that the presence of an auxiliary amine group could improve the catalytic activity of previous catalysts that resemble the oxyanion hole structure found in many enzymes. A simple modeling procedure is used to predict the catalytic activity of the tested catalyst, that in some cases shows k cat /k uncat values close to the range of values observed for many catalytic antibodies. Details are discussed in the article by L. Simón et al. on p. 4821 ff.