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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 performance 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.

SUBMITTER: Hickey DP 

PROVIDER: S-EPMC6000982 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature

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Pyrene hydrogel for promoting direct bioelectrochemistry: ATP-independent electroenzymatic reduction of N<sub>2</sub>.

Hickey David P DP   Lim Koun K   Cai Rong R   Patterson Ashlea R AR   Yuan Mengwei M   Sahin Selmihan S   Abdellaoui Sofiene S   Minteer Shelley D SD  

Chemical science 20180514 23


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 performance 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 meth  ...[more]

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