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

Enzyme activity by design: an artificial rhodium hydroformylase for linear aldehydes
Enzyme activity by design: an artificial rhodium hydroformylase for linear aldehydes
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.
1433-7851
13596-13600
Jarvis, Amanda
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Obrecht, Lorenz
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Deuss, Peter
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Laan, Wouter
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Gibson, Emma
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Wells, Peter P.
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Kamer, Paul
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Jarvis, Amanda
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Obrecht, Lorenz
cf982c46-5b77-4fad-aa61-5f50e8eeb233
Deuss, Peter
04e421bc-c060-4814-b283-4954768748d1
Laan, Wouter
a1415cfb-6efb-4709-9590-4f801f0e1499
Gibson, Emma
f646c967-fe31-4497-b65f-2f29a888ffd3
Wells, Peter P.
bc4fdc2d-a490-41bf-86cc-400edecf2266
Kamer, Paul
90e27318-9a28-459c-8fe6-f8e29458e7bf

Jarvis, Amanda, Obrecht, Lorenz, Deuss, Peter, Laan, Wouter, Gibson, Emma, Wells, Peter P. and Kamer, Paul (2017) Enzyme activity by design: an artificial rhodium hydroformylase for linear aldehydes. Angewandte Chemie - International Edition, 56 (44), 13596-13600. (doi:10.1002/anie.201705753).

Record type: Article

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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More information

Accepted/In Press date: 22 August 2017
e-pub ahead of print date: 13 September 2017
Published date: 23 October 2017

Identifiers

Local EPrints ID: 413631
URI: http://eprints.soton.ac.uk/id/eprint/413631
ISSN: 1433-7851
PURE UUID: 4603dbd6-4513-4718-b882-c3579247a555
ORCID for Peter P. Wells: ORCID iD orcid.org/0000-0002-0859-9172

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Date deposited: 30 Aug 2017 16:31
Last modified: 16 Mar 2024 05:40

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Contributors

Author: Amanda Jarvis
Author: Lorenz Obrecht
Author: Peter Deuss
Author: Wouter Laan
Author: Emma Gibson
Author: Peter P. Wells ORCID iD
Author: Paul Kamer

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