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How the Intricate Interactions between Carbon Nanotubes and Two Bilirubin Oxidases Control Direct and Mediated O2 Reduction

Abstract : Due to the lack of a valid approach in the design of electrochemical interfaces modified with enzymes for efficient catalysis, many oxidoreductases are still not addressed by electrochemistry. We report in this work an in-depth study of the interactions between two different bilirubin oxidases, (from the fungus Myrothecium verrucaria and from the bacterium Bacillus pumilus), catalysts of oxygen reduction, and carbon nanotubes bearing various surface charges (pristine, carboxylic-, and pyrene-methylamine-functionalized). The surface charges and dipole moment of the enzymes as well as the surface state of the nanomaterials are characterized as a function of pH. An original electrochemical approach allows determination of the best interface for direct or mediated electron transfer processes as a function of enzyme, nanomaterial type, and adsorption conditions. We correlate these experimental results to theoric voltammetric curves. Such an integrative study suggests strategies for designing efficient bioelectrochemical interfaces toward the elaboration of biodevices such as enzymatic fuel cells for sustainable electricity production.
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https://hal.archives-ouvertes.fr/hal-01363222
Contributor : Nadine Laffargue <>
Submitted on : Friday, September 9, 2016 - 2:42:29 PM
Last modification on : Tuesday, June 23, 2020 - 1:44:03 PM

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Ievgen Mazurenko, Karen Monsalve, Jad Rouhana, Philippe Parent, Carine Laffon, et al.. How the Intricate Interactions between Carbon Nanotubes and Two Bilirubin Oxidases Control Direct and Mediated O2 Reduction. ACS Applied Materials & Interfaces, Washington, D.C. : American Chemical Society, 2016, 8, pp. 23074-23085. ⟨10.1021/acsami.6b07355⟩. ⟨hal-01363222⟩

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