Pyrene hydrogel for promoting direct bioelectrochemistry: ATP-independent electroenzymatic reduction of N 2

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 analytic...

Full description

Saved in:
Bibliographic Details
Published in:Chemical science (Cambridge) 2018-06, Vol.9 (23), p.5172-5177
Main Authors: Hickey, David P, Lim, Koun, Cai, Rong, Patterson, Ashlea R, Yuan, Mengwei, Sahin, Selmihan, Abdellaoui, Sofiene, Minteer, Shelley D
Format: Article
Language:English
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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 O by laccase and, by immobilizing the catalytic subunit of nitrogenase (MoFe protein), to demonstrate the ATP-independent direct electroenzymatic reduction of N to NH .
ISSN:2041-6520
2041-6539
DOI:10.1039/c8sc01638k