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Fully Oriented Bilirubin Oxidase on Porphyrin-Functionalized Carbon Nanotube Electrodes for Electrocatalytic Oxygen Reduction

Authors :
Serge Cosnier
Michael Holzinger
Noémie Lalaoui
Alan Le Goff
Département de Chimie Moléculaire - Biosystèmes Electrochimiques et Analytiques (DCM - BEA)
Département de Chimie Moléculaire (DCM)
Université Joseph Fourier - Grenoble 1 (UJF)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)
Source :
Chemistry-A European Journal, Chemistry-A European Journal, Wiley-VCH Verlag, 2015, 21 (47), pp.16868-16873. ⟨10.1002/chem.201502377⟩
Publication Year :
2015
Publisher :
HAL CCSD, 2015.

Abstract

The efficient immobilization and orientation of bilirubin oxidase from Myrothecium verrucaria on multi-walled carbon nanotube electrodes by using π-stacked porphyrins as a direct electron-transfer promoter is reported. By comparing the use of different types of porphyrin, the rational effect of the porphyrin structure on both the immobilization and orientation of the enzyme is demonstrated. The best performances were obtained for protoporphyrin IX, which is the natural precursor of bilirubin. These electrodes exhibit full orientation of the enzyme, as confirmed by the observable non-catalytic redox system corresponding to the T1 copper center associated with pure Nernstian electrocatalytic behavior with high catalytic currents of almost 5 mA cm(-2) at neutral pH.

Details

Language :
English
ISSN :
09476539 and 15213765
Database :
OpenAIRE
Journal :
Chemistry-A European Journal, Chemistry-A European Journal, Wiley-VCH Verlag, 2015, 21 (47), pp.16868-16873. ⟨10.1002/chem.201502377⟩
Accession number :
edsair.doi.dedup.....9b0745096abc83768ac1ef601cd1164e
Full Text :
https://doi.org/10.1002/chem.201502377⟩