Swiss Science Concentrates

This article focuses on developing artificial enzymes that utilize pnictogen bonds, a type of non-covalent -hole interaction, which is rarely observed in biocatalysis.The researchers designed stibine-based pnictogen-bonding catalysts, interfaced with streptavidin mutants, to catalyze transfer hydrogenation reactions.The study highlights a significant increase in catalytic activity and stereoselectivity, with deep -holes on the Sb(V) center enhancing transition-state recognition by more than three orders of magnitude compared to substrate recognition.The artificial enzymes showed Michaelis-Menten kinetics, confirming their enzyme-like behavior and the potential for stereoselectivity.These findings open new possibilities for using pnictogen bonds in aqueous catalysis and demonstrate the compatibility of pnictogen-bonding interactions with complex catalytic systems, expanding the toolbox of artificial enzymes for challenging reactions.