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A Highly Active Biohybrid Catalyst for Olefin Metathesis in Water: Impact of a Hydrophobic Cavity in a β-Barrel Protein

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    A Highly Active Biohybrid Catalyst for Olefin Metathesis in Water: Impact of a Hydrophobic Cavity in a β-Barrel Protein
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    † Institute of Inorganic Chemistry, RWTH Aachen University, Landoltweg 1, D-52056 Aachen, Germany
    ‡ Department of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita 565-0871, Japan
    § Institute of Biotechnology, RWTH Aachen University, Worringer Weg 1, D-52056 Aachen, Germany
    *E-mail for T.H.: [email protected]
    *E-mail for J.O.: [email protected]
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    ACS Catalysis

    Cite this: ACS Catal. 2015, 5, 12, 7519–7522
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    https://doi.org/10.1021/acscatal.5b01792
    Published November 16, 2015
    Copyright © 2015 American Chemical Society
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    A series of Grubbs–Hoveyda type catalyst precursors for olefin metathesis containing a maleimide moiety in the backbone of the NHC ligand was covalently incorporated in the cavity of the β-barrel protein nitrobindin. By using two protein mutants with different cavity sizes and choosing the suitable spacer length, an artificial metalloenzyme for olefin metathesis reactions in water in the absence of any organic cosolvents was obtained. High efficiencies reaching TON > 9000 in the ROMP of a water-soluble 7-oxanorbornene derivative and TON > 100 in ring-closing metathesis (RCM) of 4,4-bis(hydroxymethyl)-1,6-heptadiene in water under relatively mild conditions (pH 6, T = 25–40 °C) were observed.

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    Cite this: ACS Catal. 2015, 5, 12, 7519–7522
    Click to copy citationCitation copied!
    https://doi.org/10.1021/acscatal.5b01792
    Published November 16, 2015
    Copyright © 2015 American Chemical Society
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