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

Todd K. Hyster, Livia Knörr, Thomas R. Ward, Tomislav Rovis

Research output: Contribution to journalArticle

444 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)500-503
Number of pages4
JournalScience
Volume338
Issue number6106
DOIs
StatePublished - Oct 26 2012

All Science Journal Classification (ASJC) codes

  • General

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