NDLI: Biomimetic <i>versus</i> enzymatic high-potential electrocatalytic reduction of hydrogen peroxide on a functionalized carbon nanotube electrode

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

Content Provider	Royal Society of Chemistry (RSC)
Author	Goff, Alan Le Carrière, Marie Cosnier, Serge Reuillard, Bertrand Gentil, Solène
Copyright Year	2015
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.
Starting Page	5139
Ending Page	5143
Page Count	5
File Format	HTM / HTML PDF
ISSN	20416520
Volume Number	6
Issue Number	9
Journal	Chemical Science
DOI	10.1039/c5sc01473e
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Subscribed
Subject Keyword	Electrode Hydrogen peroxide Enzyme Active site HRP Horseradish peroxidase Carbon nanotube Biomimetics Imidazole IMAX Sidewalls Protoporphyrin IX Polypyrrole Stacking (chemistry)
Content Type	Text
Resource Type	Article
Subject	Chemistry

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