Supramolecular Assembly of Artificial Metalloenzymes Based on the Dimeric Protein LmrR as Promiscuous ScaffoldBos, J., Browne, W. R., Driessen, A. J. M. & Roelfes, G., 12-Aug-2015, In : Journal of the American Chemical Society. 137, 31, p. 9796-9799 4 p.
Research output: Contribution to journal › Article › Academic › peer-review
Supramolecular anchoring of transition metal complexes to a protein scaffold is an attractive approach to the construction of artificial metalloenzymes since this is conveniently achieved by self-assembly. Here, we report a novel design for supramolecular artificial metalloenzymes that exploits the promiscuity of the central hydrophobic cavity of the transcription factor Lactococcal multidrug resistance Regulator (LmrR) as a generic binding site for planar coordination complexes that do not provide specific protein binding interactions. The success of this approach is manifested in the excellent enantioselectivities that are achieved in the Cu(II) catalyzed enantioselective Friedel-Crafts alkylation of indoles.
|Number of pages||4|
|Journal||Journal of the American Chemical Society|
|Publication status||Published - 12-Aug-2015|