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Issue 9, 2015
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Biomimetic versus enzymatic high-potential electrocatalytic reduction of hydrogen peroxide on a functionalized carbon nanotube electrode

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Abstract

We report the non-covalent functionalization of a multi-walled carbon nanotube (MWCNT) electrode with a biomimetic model of the horseradish peroxidase (HRP) active site. By modifying the MWCNT electrode surface with imidazole-modified polypyrrole, a new biomimetic complex of HRP was synthesized on the MWCNT sidewalls via the coordination of imidazole (Im) to the metal centre of iron protoporphyrin IX, affording (Im)(PP)FeIII. Compared to the pi-stacking of non-coordinated (PP)FeIII on a MWCNT electrode, the (Im)(PP)FeIII-modified MWCNT electrode exhibits higher electrocatalytic activity with an Imax = 0.52 mA cm−2 for the reduction of H2O2, accompanied by a high onset potential of 0.43 V vs. Ag/AgCl. The performances of these novel surface-confined HRP mimics were compared to those of a MWCNT electrode modified by HRP. Although the enzyme electrode displays a higher electrocatalytic activity towards H2O2 reduction, the (Im)(PP)FeIII-modified MWCNT electrode exhibits a markedly higher operational stability, retaining 63% of its initial activity after one month.

Graphical abstract: Biomimetic versus enzymatic high-potential electrocatalytic reduction of hydrogen peroxide on a functionalized carbon nanotube electrode

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Publication details

The article was received on 22 Apr 2015, accepted on 22 May 2015 and first published on 22 May 2015


Article type: Edge Article
DOI: 10.1039/C5SC01473E
Citation: Chem. Sci., 2015,6, 5139-5143
  • Open access: Creative Commons BY license
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    Biomimetic versus enzymatic high-potential electrocatalytic reduction of hydrogen peroxide on a functionalized carbon nanotube electrode

    B. Reuillard, S. Gentil, M. Carrière, A. Le Goff and S. Cosnier, Chem. Sci., 2015, 6, 5139
    DOI: 10.1039/C5SC01473E

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