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Use of Copper as a Trigger for the in Vivo Activity of E. coli Laccase CueO: A Simple Tool for Biosynthetic Purposes
Author(s) -
Decembrino Davide,
Girhard Marco,
Urlacher Vlada B.
Publication year - 2021
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.202000775
Subject(s) - laccase , chemistry , periplasmic space , copper , escherichia coli , multicopper oxidase , photochemistry , combinatorial chemistry , enzyme , biochemistry , organic chemistry , gene
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 CuSO 4 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.