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[(DPEPhos)(bcp)Cu]PF6: A General and Broadly Applicable Copper-Based Photoredox Catalyst
Published on: May 21, 2019
Probing electron pathways to multicopper oxidase copper centers reveals shortcut for enhancing oxygen reduction
Qiujuan Shen1, Thelma Barnetche1, Elise Courvoisier-Dezord1
1Aix Marseille Univ, CNRS, Centrale Med, ISM2 UMR 7313, 13397 Marseille, France.
Abstract:
Directly connected to an electrode, high potential MCOs catalyse the oxygen reduction reaction (ORR) at low overpotential with high efficiency. MCOs contain two redox centers, a near surface-located mononuclear copper (T1) oxidising a substrate and a buried trinuclear copper center (TNC) reducing dioxygen to water. Which of the two copper centers is directly wired to the electrode during the bioelectrocatalytic reduction of dioxygen is a challenging question to address. Beyond potentially improving the direct electron transfer process, the rational orientation of a high potential MCO should allow to bypass the rate-limiting internal electron transfer from T1 to TNC and enhance the ORR efficiency. Variants of a high potential fungal laccase (LAC3) isolated from Trametes sp. C30 were designed to target two opposite orientations in which the T1 copper center is either as close (T1-orientation) or as far (anti-T1 orientation) as possible from the MWCNT electrode. Analysis of the electrochemical response of these variants under different conditions allow to conclude: (1) the T1 center is the first electron acceptor in randomly adsorbed enzymes, (2) pyrene-enzyme hybrids allow for a selective wiring of T1 and TNC sites to MWCNTs and (3) anti-T1 oriented hybrids are three-fold more efficient for ORR.
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