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Issue 22, 2005
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Redox and redox-coupled processes of heme proteins and enzymes at electrochemical interfaces

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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.

Graphical abstract: Redox and redox-coupled processes of heme proteins and enzymes at electrochemical interfaces

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Publication details

The article was received on 07 Jun 2005, accepted on 11 Aug 2005 and first published on 31 Aug 2005


Article type: Invited Article
DOI: 10.1039/B507989F
Citation: Phys. Chem. Chem. Phys., 2005,7, 3773-3784
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    Redox and redox-coupled processes of heme proteins and enzymes at electrochemical interfaces

    D. H. Murgida and P. Hildebrandt, Phys. Chem. Chem. Phys., 2005, 7, 3773
    DOI: 10.1039/B507989F

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