Artificial (METALLO-) enzymes: Design and application

Conference Dates

September 24-28, 2017


The catalytic efficiency and high selectivities achieved by natural metalloenzymes are a source of inspiration for the design of novel bio inspired catalysts. A powerful approach for creating artificial metalloenzymes involves incorporating a synthetic transition metal catalysts into a biomolecular scaffold such as a protein or DNA. We have developed a new concept for the design of artificial metalloenzymes that involves creation of a novel active site at the dimer interface of the transcription factor LmrR (Lactococcal multidrug resistance Regulator) [1]. LmrR was selected as the protein scaffold because it contains an unusual large hydrophobic pocket on the dimer interface. Here, two novel classes of LmrR-based artificial metalloenzymes will be presented, involving either supramolecular anchoring of the metal complex[2] or biosynthetic incorporation of an unnatural metal binding amino acid using expanded genetic code methodology [3]. These artificial metalloenzymes have been applied successfully in catalytic asymmetric C-C bond forming and hydration reactions. Finally, our recent insights into how to design the second coordination sphere will be discussed. 1. J. Bos, F. Fusetti, A.J.M. Driessen and G. Roelfes, Angew. Chem. Int. Ed., 2012, 51, 7472-7475. 2. J. Bos, W.R. Browne, A.J.M. Driessen and G. Roelfes, J. Am. Chem. Soc., 2015, 137, 9796–9799. 3. I. Drienovská, A. Rioz-Martínez, A. Draksharapu and G. Roelfes, Chem. Sci., 2015, 6, 770-776. 4. M. Bersellini and G. Roelfes, Org. Biomol. Chem., 2017, DOI: 10.1039/C7OB00390K

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