Enzyme activity by design : an artificial rhodium hydroformylase for linear aldehydes
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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.
Jarvis , A , Obrecht , L , Deuss , P , Laan , W , Gibson , E K , Wells , P P & Kamer , P C J 2017 , ' Enzyme activity by design : an artificial rhodium hydroformylase for linear aldehydes ' Angewandte Chemie , vol Early View . DOI: 10.1002/ange.201705753
© 2017 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
Funding: Marie Curie Individual Fellowship project ArtOxiZymes to AGJ (contract no. H2020-MSCA-IF-2014-657755), EPSRC Critical mass grant ‘Clean catalysis for sustainable development’ (EP/J018139/1) and Sasol (CASE studentship to P.J.D.), EPSRC (EP/K014854/1).
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