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

Research output: Contribution to journalArticlepeer-review

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Enzyme activity by design : an artificial rhodium hydroformylase for linear aldehydes. / Jarvis, Amanda; Obrecht, Lorenz; Deuss, Peter; Laan, Wouter; Gibson, Emma K.; Wells, Peter P.; Kamer, Paul C J.

In: Angewandte Chemie, Vol. 129, No. 44, 23.10.2017, p. 13784-13788.

Research output: Contribution to journalArticlepeer-review

Harvard

Jarvis, A, Obrecht, L, Deuss, P, Laan, W, Gibson, EK, Wells, PP & Kamer, PCJ 2017, 'Enzyme activity by design: an artificial rhodium hydroformylase for linear aldehydes', Angewandte Chemie, vol. 129, no. 44, pp. 13784-13788. https://doi.org/10.1002/ange.201705753

APA

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, 129(44), 13784-13788. https://doi.org/10.1002/ange.201705753

Vancouver

Jarvis A, Obrecht L, Deuss P, Laan W, Gibson EK, Wells PP et al. Enzyme activity by design: an artificial rhodium hydroformylase for linear aldehydes. Angewandte Chemie. 2017 Oct 23;129(44):13784-13788. https://doi.org/10.1002/ange.201705753

Author

Jarvis, Amanda ; Obrecht, Lorenz ; Deuss, Peter ; Laan, Wouter ; Gibson, Emma K. ; Wells, Peter P. ; Kamer, Paul C J. / Enzyme activity by design : an artificial rhodium hydroformylase for linear aldehydes. In: Angewandte Chemie. 2017 ; Vol. 129, No. 44. pp. 13784-13788.

Bibtex - Download

@article{ad037756dba64e29b399311316bfb3e7,
title = "Enzyme activity by design: an artificial rhodium hydroformylase for linear aldehydes",
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.",
keywords = "Artificial metalloenzymes, Catalyst design, Hydroformylation, Phosphines, Rhodium",
author = "Amanda Jarvis and Lorenz Obrecht and Peter Deuss and Wouter Laan and Gibson, {Emma K.} and Wells, {Peter P.} and Kamer, {Paul C J}",
note = "Funding: Marie Curie Individual Fellowship project ArtOxiZymes to AGJ (contract no. H2020-MSCA-IF-2014-657755), EPSRC Critical mass grant {\textquoteleft}Clean catalysis for sustainable development{\textquoteright} (EP/J018139/1) and Sasol (CASE studentship to P.J.D.), EPSRC (EP/K014854/1).",
year = "2017",
month = oct,
day = "23",
doi = "10.1002/ange.201705753",
language = "English",
volume = "129",
pages = "13784--13788",
journal = "Angewandte Chemie",
issn = "0044-8249",
publisher = "John Wiley and Sons",
number = "44",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Enzyme activity by design

T2 - an artificial rhodium hydroformylase for linear aldehydes

AU - Jarvis, Amanda

AU - Obrecht, Lorenz

AU - Deuss, Peter

AU - Laan, Wouter

AU - Gibson, Emma K.

AU - Wells, Peter P.

AU - Kamer, Paul C J

N1 - 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).

PY - 2017/10/23

Y1 - 2017/10/23

N2 - 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.

AB - 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.

KW - Artificial metalloenzymes

KW - Catalyst design

KW - Hydroformylation

KW - Phosphines

KW - Rhodium

UR - http://onlinelibrary.wiley.com/doi/10.1002/ange.201705753/full#footer-support-info

U2 - 10.1002/ange.201705753

DO - 10.1002/ange.201705753

M3 - Article

VL - 129

SP - 13784

EP - 13788

JO - Angewandte Chemie

JF - Angewandte Chemie

SN - 0044-8249

IS - 44

ER -

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