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Redox and redox-coupled processes of heme proteins and enzymes at electrochemical interfaces
Citation key ISI:000232946700001
Author Murgida, D H and Hildebrandt, P
Pages 3773-3784
Year 2005
ISSN 1463-9076
Address THOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLAND
Journal Phys. Chem. Chem. Phys.
Volume 7
Number 22
Publisher ROYAL SOC CHEMISTRY
Abstract Modern bioelectrochemical methods rely upon the immobilisation of redox proteins and enzymes on electrodes coated with biocompatible materials to prevent denaturation. However, even when protein denaturation is effectively avoided, heterogeneous protein electron transfer is often coupled to non-Faradaic processes like reorientation, conformational transitions or acid-base equilibria. Disentangling these processes requires methods capable of probing simultaneously the structure and reaction dynamics of the adsorbed species. Here we provide an overview of the recent developments in Raman and infrared surface-enhanced spectroelectrochemical techniques applied to the study of soluble and membrane bound redox heme proteins and enzymes. Possible biological implications of the findings are critically discussed.
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