Cofactor Binding Dynamics Influence the Catalytic Activity and Selectivity of an Artificial MetalloenzymeVillarino, L., Chordia, S., Alonso-Cotchico, L., Reddem, E., Zhou, Z., Thunnissen, A. M. W. H., Maréchal, J-D. & Roelfes, G., 18-Sep-2020, In : ACS Catalysis. 10, 20, p. 11783-11790 8 p.
Research output: Contribution to journal › Article › Academic › peer-review
We present an artificial metalloenzyme based on the transcriptional regulator LmrR that exhibits dynamics involving the positioning of its abiological metal cofactor. The position of the cofactor, in turn, was found to be related to the preferred catalytic reactivity, which is either the enantioselective Friedel-Crafts alkylation of indoles with β-substituted enones or the tandem Friedel-Crafts alkylation/enantioselective protonation of indoles with α-substituted enones. The artificial metalloenzyme could be specialized for one of these catalytic reactions introducing a single mutation in the protein. The relation between cofactor dynamics and activity and selectivity in catalysis has not been described for natural enzymes and, to date, appears to be particular for artificial metalloenzymes.
|Number of pages||8|
|Publication status||Published - 18-Sep-2020|
- artificial metalloenzymes, biocatalysis, structural dynamics, enzyme design, copper