|According to a research study published by the Royal Society of Chemistry, reprogramming the genetic code of bacteria to incorporate an unnatural amino acid enabled University of Groningen scientists to create a new metalloenzyme capable of catalysing an enantioselective reaction. Metalloenzymes combine the flexibility of metal catalysts with the high activity and selectivity of enzymes. Artificial metalloenzymes are produced by inserting a catalytically active transition metal complex into a biomolecular scaffold, like a protein.
The research team led by Gerard Roelfes, from the University of Groningen, Netherlands, engineered Escherichia coli cells to include a copper-binding amino acid into one of its proteins, without the need for any further chemical modification or purification steps. The resulting me-talloenzyme was tested on a catalytic asymmetric Friedel–Crafts alkylation reaction, achieving an enantiomeric excess of upto 83%. The group is now looking to develop new artificial metalloenzymes with the capability to perform chemistry that traditional transition metal catalysts cannot.