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Synfacts 2013; 9(1): 0065
DOI: 10.1055/s-0032-1317748
Metal-Catalyzed Asymmetric Synthesis and Stereoselective Reactions
© Georg Thieme Verlag Stuttgart · New York

Artificial Rh(III)–Metalloenzyme-Catalyzed Asymmetric C–H Activation

Contributor(s):
Mark Lautens
,
Lei Zhang
Hyster TK, Knörr L, Ward TR, * Rovis T. * Colorado State University, Fort Collins, USA and University of Basel, Switzerland
Biotinylated Rh(III) Complexes in Engineered Streptavidin for Accelerated Asymmetric C–H Activation.

Science 2012;
338: 500−503
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Further Information

Publication History

Publication Date:
17 December 2012 (online)

 
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Key words

rhodium - streptavidin - biotin - artificial metalloenzymes - benzamides - dihydroisoquinolines - asymmetric C–H activation

Significance

A highly active, artificial rhodium(III) metalloenzyme that catalyzes an asymmetric synthesis of dihydroisoquinolones through C–H activation is reported. A biotinylated rhodium(III) complex is successfully incorporated into streptavidin. With active-site mutagenesis, the engineered enzyme displayed up to 100-fold reaction rate increase compared to the activity of the unbound rhodium complex.


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Comment

As Cp is the only permanently bound ligand on rhodium in the catalytic cycle, it has been difficult to render this reaction enantioselective until recently. This report provides an alternative solution for this problem. Based on the concerted metalation–deprotonation mechanism, the authors used docking modeling and introduced a basic carboxylate moiety in the active site. With kinetic isotope effect experiments, the importance of this mutation in accelerating the catalysis is demonstrated.


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