Name: | Description: | Size: | Format: | |
---|---|---|---|---|
228.85 KB | Adobe PDF |
Advisor(s)
Abstract(s)
"Electrochemical mediators transfer redox equivalents between the active sites of
enzymes and electrodes and, in this way, trigger bioelectrocatalytic redox
processes. This has been very useful in the development of the so-called second
generation biosensors, where they are able to transduce the catalytic event into an
electrical signal. Among other pre-requisites, redox mediators must be readily
oxidized/reduced at the electrode surface and easily interact with the
biorecognition component. Small chemical compounds (e.g. ferrocene derivatives,
ruthenium or osmium complexes and viologens) are frequently used for this
purpose, but lately, small redox proteins (e.g. horse heart cytochrome c) have also
played the role of redox partners in biosensing applications. In general, the
docking between two complementary proteins introduces a second level of
selectivity to the biosensor and enlarges the list of compounds targeted for
analysis. Moreover, electrochemical interferences are frequently minimized owing
to the small overpotentials achieved. This paper aims to provide an overview of
enzyme biosensors that are mediated by electron transfer proteins. The article
begins with a few considerations on mediated electrochemistry in biosensing
2
systems and proceeds with a detailed description of relevant works concerning the
cooperative use of redox enzymes and biological electron donors/acceptors."
Description
The final publication is available at Springer.
Keywords
Electrochemical biosensors Redox partner Electron transfer protein Mediated electrochemistry
Citation
Original source: Analytical and Bioanalytical Chemistry. April 2013, Volume 405, Issue 11, pp 3619-3635