Structural highlights
Publication Abstract from PubMed
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 beta-substituted enones or the tandem Friedel-Crafts alkylation/enantioselective protonation of indoles with alpha-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.
Cofactor Binding Dynamics Influence the Catalytic Activity and Selectivity of an Artificial Metalloenzyme.,Villarino L, Chordia S, Alonso-Cotchico L, Reddem E, Zhou Z, Thunnissen AMWH, Marechal JD, Roelfes G ACS Catal. 2020 Oct 16;10(20):11783-11790. doi: 10.1021/acscatal.0c01619. Epub, 2020 Sep 18. PMID:33101759[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Villarino L, Chordia S, Alonso-Cotchico L, Reddem E, Zhou Z, Thunnissen AMWH, Marechal JD, Roelfes G. Cofactor Binding Dynamics Influence the Catalytic Activity and Selectivity of an Artificial Metalloenzyme. ACS Catal. 2020 Oct 16;10(20):11783-11790. doi: 10.1021/acscatal.0c01619. Epub, 2020 Sep 18. PMID:33101759 doi:http://dx.doi.org/10.1021/acscatal.0c01619
