Methanol-Driven Oxidative Rearrangement of Biogenic Furans - Enzyme Cascades vs. Photobiocatalysis.

Christina Jäger,Cloé Bruneau,Philip K Wagner,Jan Deska,Martin H G Prechtl

doi:10.3389/fchem.2021.635883

Abstract

The oxidative ring expansion of bio-derived furfuryl alcohols to densely functionalized six-membered O-heterocycles represents an attractive strategy in the growing network of valorization routes to synthetic building blocks out of the lignocellulosic biorefinery feed. In this study, two scenarios for the biocatalytic Achmatowicz-type rearrangement using methanol as terminal sacrificial reagent have been evaluated, comparing multienzymatic cascade designs with a photo-bio-coupled activation pathway.

Highlights

Since its discovery in the early 1970’s (Achmatowicz et al, 1971; Lefebvre, 1972), the Achmatowicz rearrangement has gained substantial recognition by the synthetic community (Deska et al, 2015) and has found versatile applications in the preparation of complex heterocyclic target structures (Ghosh and Brindisi, 2016; Blume et al, 2016; Naapuri et al, 2017)
Utilizing furfuryl alcohols as the basic starting point of the ring expansion strategy to substituted hydroxypyranones, in recent years this oxidative rearrangement has attracted substantial interest as a potentially valuable tool for future value chains based on lignocellulosic biomass, where the furfural platform represents a key component in the endeavor to create value chains that are independent on fossil resources (Mariscal, 2016; Kabbour and Luque, 2020)
We have investigated two complementary pathways for the enzymatic ring rearrangement of biogenic furfuryl alcohols based on methanol-driven hydrogen peroxide generation modules a) via a multi-enzymatic route and b) in a photobio-coupled scenario

Summary

Introduction

Since its discovery in the early 1970’s (Achmatowicz et al, 1971; Lefebvre, 1972), the Achmatowicz rearrangement has gained substantial recognition by the synthetic community (Deska et al, 2015) and has found versatile applications in the preparation of complex heterocyclic target structures (Ghosh and Brindisi, 2016; Blume et al, 2016; Naapuri et al, 2017). The oxygen-transfer biocatalyst is supplemented by glucose oxidase (GOx) to provide the necessary hydrogen peroxide via reduction of air. This protocol has been proven to be highly effective, and has been implemented into synthetic applications (Blume et al, 2016) and biocatalytic cascades (Liu et al, 2018), we have pursued the search for alternative aerobic activation routes in order to substitute the glucose, on one side to create complementary sacrificial agents for the design of more complex biocascades, and due to the somewhat poor atom-economy of the glucose.

Methods

Results

Conclusion