Enzyme Activity by Design: An Artificial Rhodium Hydroformylase for Linear Aldehydes

Artificial metalloenzymes are hybrid catalysts that offer a unique opportunity to combine the superior performance of natural protein structures with the unnatural reactivity of transition metal catalytic centers. They provide the prospect of highly selective and active catalytic chemical conversions for which natural enzymes are unavailable. Here we show that by rationally combining robust site-specific phosphine bioconjugation methodology and a lipid-binding protein (SCP-2L), an artificial rhodium hydroformylase can be developed that displays remarkable activities and selectivities for the biphasic production of long chain linear aldehydes under aqueous conditions. This study demonstrates that judiciously chosen protein binding scaffolds can be adapted to obtain metalloenzymes that provide the reactivity of the introduced metal center combined with specifically intended product selectivity.