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Enzyme activity by design: an artificial rhodium hydroformylase for linear aldehydes

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Amanda Jarvis, Lorenz Obrecht, Peter Deuss, Wouter Laan, Emma K. Gibson, Peter P. Wells, Paul C J Kamer

School/Research organisations


Artificial metalloenzymes (ArMs) 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. Therefore, they provide the prospect of highly selective and active catalytic chemical conversions for which natural enzymes are unavailable. Herein, we show how by rationally combining robust site-specific phosphine bioconjugation methods and a lipid-binding protein (SCP-2L), an artificial rhodium hydroformylase was developed that displays remarkable activities and selectivities for the biphasic production of long-chain linear aldehydes under benign aqueous conditions. Overall, 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.


Original languageEnglish
Pages (from-to)13784-13788
JournalAngewandte Chemie
Issue number44
Early online date13 Sep 2017
Publication statusPublished - 23 Oct 2017

    Research areas

  • Artificial metalloenzymes, Catalyst design, Hydroformylation, Phosphines, Rhodium

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