Oxalate Oxidase for In Situ H2O2-generation in Unspecific Peroxygenase-Catalysed Drug Oxyfunctionalisations

Gideon James Grogan, Elvira Romero, Magnus Johansson, Jared Cartwright, Martin A Hayes

Research output: Contribution to journalArticlepeer-review


H2O2-driven enzymes are of great interest for industrial
biotransformations. Herein, we show for the first time that oxalate
oxidase (OXO) is an efficient in situ source of H2O2 for one of these
biocatalysts, which is known as unspecific peroxygenase (UPO). OXO
is reasonably robust, produces only CO2 as a by-product and uses
oxalate as a cheap sacrificial electron donor. UPO has significant
potential as an industrial catalyst for selective C-H
oxyfunctionalisations, as we confirm herein by testing a diverse drug
panel using miniaturised high-throughput assays and mass
spectrometry. 33 out of 64 drugs were converted in 5 μL-scale
reactions by the UPO with OXO (conversion >70% for 11 drugs).
Furthermore, oxidation of the drug tolmetin was achieved on a 50 mg
scale (TONUPO 25,664) with 84% yield, which was further improved
via enzyme immobilization. This one-pot approach ensures adequate
H2O2 levels, enabling rapid access to industrially relevant molecules
that are difficult to obtain by other routes.
Original languageEnglish
Article number e202207831
Number of pages7
JournalAngewandte Chemie International Edition
Early online date2 Aug 2022
Publication statusE-pub ahead of print - 2 Aug 2022

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