Abstract
Despite their recognised excellence for observing and analyzing the redox thermodynamics and kinetics of small molecule systems, voltammetric methods are relatively unfamiliar tools for investigating redox centres in proteins. Prior to breakthroughs achieved in the 1970s, it was widely believed that proteins were able to undergo facile direct (unmediated) electron exchange with an electrode [1]. Presumed complications in applying direct electrochemical methods, i.e. irreversible adsorption with denaturation, and sluggish electrode kinetics due to the protein’s occluded active site(s), appeared serious obstacles to progress, and interest was focused instead on indirectmethods of electrochemical measurement. Thus potentiometry, with employment of small redox mediators to facilitate electrochemical equilibration during spectroscopically monitored titrations of redox centres, has become the established way to determine reduction potentials [2]. The first studies to demonstrate conclusively that voltammetry might be as viable for Proteins (MW > 01 kDa) as for small molecules were carried out with cytochromes. Nikki and co-workers found that cytochrome c3, an active and robust electron-controlled electrochemistry at a mercury electrode [3], while the research groups of Hill and Kuwana independently achieved reversible, diffusion-controlled electrochemistry of mitochemical cytochrome c, respectivey at 4,4′-bipyridyl modified gold and at metal oxide electrodes [4, 5].
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Armstrong, F.A. (1997). Applications of voltammetric methods for probing the chemistry of redox proteins. In: Lenaz, G., Milazzo, G. (eds) Bioelectrochemistry of Biomacromolecules. Bioelectrochemistry: Principles and Practice, vol 5. Birkhäuser Basel. https://doi.org/10.1007/978-3-0348-9179-0_4
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