10.1021/ja067840j.s001
Chad A. Lewis
Chad A.
Lewis
Anna Chiu
Anna
Chiu
Michele Kubryk
Michele
Kubryk
Jaume Balsells
Jaume
Balsells
David Pollard
David
Pollard
Craig K. Esser
Craig K.
Esser
Jerry Murry
Jerry
Murry
Robert A. Reamer
Robert A.
Reamer
Karl B. Hansen
Karl B.
Hansen
Scott J. Miller
Scott J.
Miller
Remote Desymmetrization at Near-Nanometer Group Separation Catalyzed by
a Miniaturized Enzyme Mimic
American Chemical Society
2006
chiral catalysts
Miniaturized Enzyme MimicThe chirality
enzyme
enantiotopic sites increases
catalysis addresses enantioselective synthesis
complexity
effect stereospecific reactions
2006-12-27 00:00:00
Journal contribution
https://acs.figshare.com/articles/journal_contribution/Remote_Desymmetrization_at_Near_Nanometer_Group_Separation_Catalyzed_by_a_Miniaturized_Enzyme_Mimic/3038626
The chirality of biological receptors often requires syntheses of therapeutic compounds in single enantiomer form. The field of asymmetric catalysis addresses enantioselective synthesis with chiral catalysts. Chemical differentiation of sites within molecules that are separated in space by long distances presents special challenges to chiral catalysts. As the distance between enantiotopic sites increases within a substrate, so too may the requirements for size and complexity for the catalyst. The extreme of catalyst complexity could be defined by macromolecular enzymes and their amazing capacity to effect stereospecific reactions over long distances between reactive sites and enzyme−substrate contacts. We report here a synthetic, miniaturized enzyme mimic that catalyzes a desymmetrization reaction over a very long distance.