Enzymatic aerobic ring rearrangement of optically active furylcarbinols

Daniel Thiel, Diana Doknić and Jan Deska ()
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Daniel Thiel: Universität zu Köln
Diana Doknić: Universität zu Köln
Jan Deska: Universität zu Köln

Nature Communications, 2014, vol. 5, issue 1, 1-7

Abstract: Abstract Biogenic furans are currently discussed as highly attractive alternative feedstock in a post-fossil society; thus, also the creation of sustainable furan valorization pathways appears of great importance. Here an artificial Achmatowicz monooxygenase activity for the aerobic ring expansion of furans is achieved by the combination of commercial glucose oxidase as oxygen-activating biocatalyst and wild-type chloroperoxidase as oxygen-transfer mediator, providing a biological ready-to-use solution for this truly synthetic furan rearrangement. In concert with enzymatic transformations for the enantioselective preparation of optically active furylcarbinols, purely biocatalytic reaction cascades for the stereocontrolled construction of complex pyranones are obtained, exhibiting high functional group tolerance even to oxidation-sensitive moieties.

Date: 2014
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms6278

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DOI: 10.1038/ncomms6278

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