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Dynamics of Metal Complex Binding in Relation to Catalytic Activity and Selectivity of an Artificial Metalloenzyme

preprint
submitted on 11.03.2020 and posted on 12.03.2020 by Lara Villarino, Shreyans Chordia, Lur Alonso-Cotchico, Eswar R. Reddem, Andy-Mark Thunnissen, Jean-Didier Maréchal, Gerard Roelfes
We present an artificial metalloenzyme based on the transcriptional regulator LmrR that exhibits a unique form of structural dynamics involving the positioning of its abiological cofactor. The position of the cofactor was found to relate to the preferred catalytic activity, which is either the enantioselective Friedel-Crafts alkylation of indoles with beta-substituted indoles or the tandem Friedel-Crafts alkylation / enantioselective protonation of indoles with alpha-substituted enones. The artificial metalloenzyme could be specialized for one of these reactions by introducing a single mutation in the protein.

Funding

European Research Council, grant no. 280010

Netherlands Organisation for Scientific Research, grant no. 724.013.003

Xunta de Galicia, Plan I2C

Ministry of Education, Culture and Science, grant no. 024.001.035

Spanish MINECO, CTQ2017-87889-P

History

Email Address of Submitting Author

j.g.roelfes@rug.nl

Institution

University of Groningen, Stratingh Institute for Chemistry

Country

the Netherlands

ORCID For Submitting Author

0000-0002-0364-9564

Declaration of Conflict of Interest

no conflict of interest

Version Notes

this is the first (original) submission

Exports