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Issue 10, 2012
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Spectroscopic analysis of immobilised redox enzymes under direct electrochemical control

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Abstract

This article reviews recent developments in spectroscopic analysis of electrode-immobilised enzymes under direct, unmediated electrochemical control. These methods unite the suite of spectroscopic methods available for characterisation of structural, electronic and coordination changes in proteins with the exquisite control over complex redox enzymes that can be achieved in protein film electrochemistry in which immobilised protein molecules exchange electrons directly with an electrode. This combination is particularly powerful in studies of highly active enzymes where redox states can be controlled even under fast electrocatalytic turnover. We examine examples in which UV-visible, IR, Raman and MCD spectroscopy have been combined with direct electrochemistry to probe redox-dependent chemistry, and consider future opportunities for ‘direct’ spectroelectrochemistry of immobilised enzymes.

Graphical abstract: Spectroscopic analysis of immobilised redox enzymes under direct electrochemical control

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Article information


Submitted
21 Sep 2011
Accepted
24 Oct 2011
First published
07 Nov 2011

Chem. Commun., 2012,48, 1400-1409
Article type
Feature Article

Spectroscopic analysis of immobilised redox enzymes under direct electrochemical control

P. A. Ash and K. A. Vincent, Chem. Commun., 2012, 48, 1400 DOI: 10.1039/C1CC15871F

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