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- W2516051147 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." @default.
- W2516051147 created "2016-09-16" @default.
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- W2516051147 date "2016-08-25" @default.
- W2516051147 modified "2023-10-15" @default.
- W2516051147 title "How the Intricate Interactions between Carbon Nanotubes and Two Bilirubin Oxidases Control Direct and Mediated O<sub>2</sub> Reduction" @default.
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- W2516051147 doi "https://doi.org/10.1021/acsami.6b07355" @default.
- W2516051147 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27533778" @default.
- W2516051147 hasPublicationYear "2016" @default.
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