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

Research output: Contribution to journalArticlepeer-review

Author(s)

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

School/Research organisations

Abstract

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.
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Details

Original languageEnglish
Pages (from-to)13784-13788
JournalAngewandte Chemie
Volume129
Issue number44
Early online date13 Sep 2017
DOIs
Publication statusPublished - 23 Oct 2017

    Research areas

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

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