Use of Copper as a Trigger for the in Vivo Activity of E. coli Laccase CueO: A Simple Tool for Biosynthetic Purposes. (4th February 2021)

• Record Type: Journal Article
• Authors: Decembrino, Davide; Girhard, Marco; Urlacher, Vlada B.
• Is Part Of: Chembiochem. Volume 22:Number 8(2021)
• Page Start: 1470
• Page End: 1479
• Publication Date: 2021-02-04
• Subjects: biotransformation -- CueO -- enzymes -- laccase -- phenolic coupling; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.202000775
• Languages: English
• ISSNs: 1439-4227

Abstract

Abstract: Laccases are multi‐copper oxidases that catalyze the oxidation of various electron‐rich substrates with concomitant reduction of molecular oxygen to water. The multi‐copper oxidase/laccase CueO of Escherichia coli is responsible for the oxidation of Cu + to the less harmful Cu 2+ in the periplasm. CueO has a relatively broad substrate spectrum as laccase, and its activity is enhanced by copper excess. The aim of this study was to trigger CueO activity in vivo for the use in biocatalysis. The addition of 5 mM CuSO4 was proven effective in triggering CueO activity at need with minor toxic effects on E. coli cells. Cu‐treated E. coli cells were able to convert several phenolic compounds to the corresponding dimers. Finally, the endogenous CueO activity was applied to a four‐step cascade, in which coniferyl alcohol was converted to the valuable plant lignan (−)‐matairesinol. Abstract : Simple and efficient : The endogenous E. coli laccase CueO was activated by the addition of copper ions to cells, which were subsequently used for oxidative phenolic coupling. As a proof of concept, CueO‐catalyzed dimerization of coniferyl alcohol was integrated into a multi‐enzyme cascade in E. coli to produce the plant lignan (−)‐matairesinol.