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Pyrene Hydrogel for Promoting Direct Bioelectrochemistry: ATP-Independent Electroenzymatic Reduction of N2

Abstract

Enzymatic bioelectrocatalysis often requires an artificial redox mediator to observe significant electron transfer rates. The use of such mediators can add a substantial overpotential and obfuscate the protein’s native kinetics, which limits the voltage of a biofuel cell and alters the analytical peformance of biosensors. Herein, we describe a material for facilitating direct electrochemical communication with redox proteins based on a novel pyrene-modified linear poly(ethyleneimine). This method was applied for promoting direct bioelectrocatalytic reduction of O2 by laccase and, by immobilizing the catalytic subunit of nitrogenase (MoFe protein), to demonstrate the ATP-independent direct electroenzymatic reduction of N2 to NH3.

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Publication details

The article was received on 10 Apr 2018, accepted on 13 May 2018 and first published on 14 May 2018


Article type: Edge Article
DOI: 10.1039/C8SC01638K
Citation: Chem. Sci., 2018, Accepted Manuscript
  • Open access: Creative Commons BY-NC license
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    Pyrene Hydrogel for Promoting Direct Bioelectrochemistry: ATP-Independent Electroenzymatic Reduction of N2

    D. P. Hickey, K. Lim, R. Cai, A. Patterson, M. Yuan, S. Sahin, S. Abdellaoui and S. Minteer, Chem. Sci., 2018, Accepted Manuscript , DOI: 10.1039/C8SC01638K

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