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Model-Driven Design of Redox Mediators: Quantifying the Impact of Quinone Structure on Bioelectrocatalytic Activity with Glucose Oxidase. | LitMetric

Model-Driven Design of Redox Mediators: Quantifying the Impact of Quinone Structure on Bioelectrocatalytic Activity with Glucose Oxidase.

J Phys Chem B

Department of Chemical Engineering & Materials Science, Michigan State University, East Lansing, Michigan 48824, United States.

Published: September 2023

AI Article Synopsis

  • * The study identifies key structure-function relationships in redox mediators, focusing on their redox potential and molecular area to predict effectiveness in electroenzymatic systems.
  • * Advanced techniques like rapid scan stopped-flow spectrophotometry were used to analyze the reactions between quinones and glucose oxidase, enhancing our understanding of how the structure of quinones affects electron transfer in these reactions.

Article Abstract

Successful application of emerging bioelectrocatalysis technologies depends upon an efficient electrochemical interaction between redox enzymes as biocatalysts and conductive electrode surfaces. One approach to establishing such enzyme-electrode interfaces utilizes small redox-active molecules to act as electron mediators between an enzyme-active site and the electrode surface. While redox mediators have been successfully used in bioelectrocatalysis applications ranging from enzymatic electrosynthesis to enzymatic biofuel cells, they are often selected using a guess-and-check approach. Herein, we identify structure-function relationships in redox mediators that describe the bimolecular rate constant for its reaction with a model enzyme, glucose oxidase (GOx). Based on a library of quinone-based redox mediators, a quantitative structure-activity relationship (QSAR) model is developed to describe the importance of mediator redox potential and projected molecular area as two key parameters for predicting the activity of quinone/GOx-based electroenzymatic systems. Additionally, rapid scan stopped-flow spectrophotometry was used to provide fundamental insights into the kinetics and the stoichiometry of reactions between different quinones and the flavin adenine dinucleotide (FAD/FADH) cofactor of GOx. This work provides a critical foundation for both designing new enzyme-electrode interfaces and understanding the role that quinone structure plays in altering electron flux in electroenzymatic reactions.

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Source
http://dx.doi.org/10.1021/acs.jpcb.3c03740DOI Listing

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