A Metal Ion Regulated Artificial Metalloenzyme
Regulation of enzyme activity is essential in living cells. The rapidly increasing number of designer enzymes with new-to-nature activities makes it necessary to develop novel strategies for controlling their catalytic activity. Here we present the development of a metal ion regulated artificial metalloenzyme created by combining two anchoring strategies, covalent and supramolecular, for introducing a regulatory and a catalytic site, respectively. This artificial metalloenzyme is activated in the presence of Fe2+ ions, but only marginally in the presence of Zn2+.
An Artificial Heme Enzyme for Cyclopropanation Reactions
An Enantioselective Artificial Metallo-Hydratase
Direct addition of water to alkenes to generate important chiral alcohols as key motif in a variety of natural products still remains a challenge in organic chemistry. Here, we report the first enantioselective artificial metallo-hydratase, based on the transcription factor LmrR, which catalyses the conjugate addition of water to generate chiral β-hydroxy ketones with enantioselectivities up to 84% ee. A mutagenesis study revealed that an aspartic acid and a phenylalanine located in the active site play a key role in achieving efficient catalysis and high enantioselectivities.
Artificial Metalloenzymes for Asymmetric Catalysis by Creation of Novel Active Sites in Protein and DNA ScaffoldsReview
Artificial Metalloenzymes for Enantioselective CatalysisReview
Design of an Enantioselective Artificial Metallo-Hydratase Enzyme Containing an Unnatural Metal-Binding Amino Acid
Enantioselective Artificial Metalloenzymes by Creation of a Novel Active Site at the Protein Dimer Interface
Hybrid Catalysts as Lewis AcidReview
LmrR: A Privileged Scaffold for Artificial MetalloenzymesReview