Comprehensive Study of the Enzymatic Catalysis of the Electrochemical Oxygen Reduction Reaction (ORR) by Immobilized Copper Efflux Oxidase (CueO) From Escherichia coli

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Title: Comprehensive Study of the Enzymatic Catalysis of the Electrochemical Oxygen Reduction Reaction (ORR) by Immobilized Copper Efflux Oxidase (CueO) From Escherichia coli
Authors: Chumillas, Sara | Maestro, Beatriz | Feliu, Juan M. | Climent, Victor
Research Group/s: Electroquímica de Superficies
Center, Department or Service: Universidad de Alicante. Departamento de Química Física | Universidad de Alicante. Instituto Universitario de Electroquímica
Keywords: Bioelectrocatalysis | CueO | Protein voltammetry | Oxygen reduction reaction | Laccase
Knowledge Area: Química Física
Issue Date: 24-Aug-2018
Publisher: Frontiers Media
Citation: Chumillas S, Maestro B, Feliu JM and Climent V (2018) Comprehensive Study of the Enzymatic Catalysis of the Electrochemical Oxygen Reduction Reaction (ORR) by Immobilized Copper Efflux Oxidase (CueO) From Escherichia coli. Front. Chem. 6:358. doi: 10.3389/fchem.2018.00358
Abstract: In recent years, enzymatic fuel cells have experienced a great development promoted by the availability of novel biological techniques that allow the access to a large number of enzymatic catalysts. One of the most important aspects in this area is the development of biocatalysts for the oxygen reduction reaction (ORR). Laccases from the group of enzymes called blue multi-cooper oxidases have received considerable attention because of their ability to catalyze the electrochemical oxygen reduction reaction to water when immobilized on metallic or carbonaceous electrode materials. In this paper we report a comprehensive study of the electrocatalytic activity of the enzyme Copper efflux oxidase (CueO) from Escherichia coli immobilized on different electrode materials. The influence of the electrode substrate employed for protein immobilization was evaluated using glassy carbon, gold or platinum electrodes. Gold and platinum electrodes were modified using different self-assembled monolayers (SAM) able to tune the electrostatic interaction between the protein and the substrate, depending on the nature of the terminal functional group in the SAM. The effects of protein immobilization time, electrode potential, solution pH and temperature, protein and O2 concentration have been carefully investigated. Finally, direct electron transfer (DET) was investigated in the presence of the following inhibitors: fluoride (F−), chloride (Cl−) and azide (N−3).
Sponsor: The authors thankfully acknowledge financial support from the Ministerio de Economia, Industria y Competitividad (CTQ2010–18570 and CTQ2016-76221-P). SC thanks the University of Alicante for the grant UAFPU2013-5796.
URI: http://hdl.handle.net/10045/78349
ISSN: 2296-2646
DOI: 10.3389/fchem.2018.00358
Language: eng
Type: info:eu-repo/semantics/article
Rights: © 2018 Chumillas, Maestro, Feliu and Climent. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
Peer Review: si
Publisher version: https://doi.org/10.3389/fchem.2018.00358
Appears in Collections:INV - EQSUP - Artículos de Revistas

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