Probing biological redox chemistry with large amplitude Fourier transformed ac voltammetry.

Hope Adamson,Alison Parkin,Alan M Bond

doi:10.1039/c7cc03870d

Abstract

Biological electron-exchange reactions are fundamental to life on earth. Redox reactions underpin respiration, photosynthesis, molecular biosynthesis, cell signalling and protein folding. Chemical, biomedical and future energy technology developments are also inspired by these natural electron transfer processes. Further developments in techniques and data analysis are required to gain a deeper understanding of the redox biochemistry processes that power Nature. This review outlines the new insights gained from developing Fourier transformed ac voltammetry as a tool for protein film electrochemistry.

Highlights

Biological redox reactions are mediated by both small and large molecules, ranging from species such as quinones, which resemble typical synthetic chemistry redox reagents, to complex metalloenzymes comprising ‘‘wires’’ of redox-active centers.[1]
This review focuses on redox active proteins and enzymes, and the new mechanistic insights which can be gained by integrating the technique of large amplitude Fourier transformed voltammetry[4] (FTacV) into the toolbox of protein film electrochemistry
This review aims to illustrate the limitations which arise from using conventional dc voltammetry in protein film electrochemistry (PFE), and exemplify the more powerful insight which can be gained from the development of protein film large amplitude Fourier transformed alternating current voltammetry (PF-Fourier transformed ac voltammetry (FTacV))

Summary

Introduction

Biological redox reactions are mediated by both small and large molecules, ranging from species such as quinones, which resemble typical synthetic chemistry redox reagents, to complex metalloenzymes comprising ‘‘wires’’ of redox-active centers (i.e. cytochrome c oxidase, the enzyme responsible for converting O2 to H2O in the mitochondria of all human cells, see Fig. 1).[1]. Techniques to study redox proteins and enzymes. The redox-active molecular centers within a protein or enzyme can comprise amino acids, organic cofactors or transition metal active sites.[7] Insight into the structural configuration of these centers can be provided via a number of techniques, with protein crystallography providing an invaluable ‘‘big picture’’ 3-D map of the whole structure that is useful for relating evolutionary sequence changes to alterations in biochemical function. Modern molecular biology techniques have largely overcome the historic challenges inherent in producing enough pure protein/enzyme for crystallographic trials, and Feature Article

Objectives

Methods

Conclusion