Skip to Main content Skip to Navigation
Journal articles

Efficiency of site-specific clicked laccase-carbon nanotubes biocathodes towards O2 reduction

Abstract : A maximization of a direct electron transfer (DET) between redox enzymes and electrodes can be obtained through the oriented immobilization of enzymes onto an electroactive surface. Here, we present a strategy for obtaining carbon nanotube (CNTs) based electrodes covalently modified with perfectly control-oriented fungal laccases. Modelisations of the laccase-CNT interaction and of electron conduction pathways serve as guide in choosing grafting positions. Homogeneous populations of alkyne-modified laccases are obtained via the reductive amination of a unique surface accessible lysine residue selectively engineered near either one or the other of the two copper centers in enzyme variants. Immobilization of the site-specific alkynated enzymes is achieved via copper click on azido-modified CNTs. A highly efficient reduction of O 2 at low overpotential and catalytic current densities over-3 mA cm −2 are obtained by minimizing the distance from the electrode surface to the trinuclear cluster.
Complete list of metadata

Cited literature [56 references]  Display  Hide  Download

https://hal.archives-ouvertes.fr/hal-02470862
Contributor : Renaud Hardré Connect in order to contact the contributor
Submitted on : Friday, February 7, 2020 - 3:38:33 PM
Last modification on : Thursday, May 26, 2022 - 3:52:20 AM
Long-term archiving on: : Friday, May 8, 2020 - 4:39:00 PM

File

Gentil_et_al-2020-Chemistry_-_...
Files produced by the author(s)

Identifiers

Collections

Citation

Solène Gentil, Pierre Rousselot-Pailley, Ferran Sancho, Viviane Robert, Yasmina Mekmouche, et al.. Efficiency of site-specific clicked laccase-carbon nanotubes biocathodes towards O2 reduction. Chemistry - A European Journal, Wiley-VCH Verlag, 2020, 26 (21), pp.4798-4804. ⟨10.1002/chem.201905234⟩. ⟨hal-02470862⟩

Share

Metrics

Record views

40

Files downloads

118