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Biotinylated Rh(III) complexes in engineered streptavidin for accelerated asymmetric C-H activation

Hyster, Todd K. and Knoerr, Livia and Ward, Thomas R. and Rovis, Tomislav. (2012) Biotinylated Rh(III) complexes in engineered streptavidin for accelerated asymmetric C-H activation. Science, 338 (6106). pp. 500-503.

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Official URL: http://edoc.unibas.ch/dok/A6070732

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Abstract

Enzymes provide an exquisitely tailored chiral environment to foster high catalytic activities and selectivities, but their native structures are optimized for very specific biochemical transformations. Designing a protein to accommodate a non-native transition metal complex can broaden the scope of enzymatic transformations while raising the activity and selectivity of small-molecule catalysis. Here, we report the creation of a bifunctional artificial metalloenzyme in which a glutamic acid or aspartic acid residue engineered into streptavidin acts in concert with a docked biotinylated rhodium(III) complex to enable catalytic asymmetric carbon-hydrogen (C–H) activation. The coupling of benzamides and alkenes to access dihydroisoquinolones proceeds with up to nearly a 100-fold rate acceleration compared with the activity of the isolated rhodium complex and enantiomeric ratios as high as 93:7.
Faculties and Departments:05 Faculty of Science > Departement Chemie > Chemie > Bioanorganische Chemie (Ward)
UniBasel Contributors:Ward, Thomas R. R. and Knörr, Livia
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Association for the Advancement of Science
ISSN:0036-8075
e-ISSN:1095-9203
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:24 Apr 2017 10:06
Deposited On:24 May 2013 09:03

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