Oriented immobilization of a fully active monolayer of histidine-tagged recombinant laccase on modified gold electrodes.
The formation of a dense monolayer of histidine-tagged recombinant laccase on gold electrodes by using a short thiol-NTA linker is described, as well as a kinetic analysis of the process by cyclic voltammetry. From a detailed analysis of the catalytic reduction of dioxygen by laccase in the presence of a one-electron redox mediator it can be concluded that the immobilized enzyme remains as active as in homogeneous solution.
Balland
Véronique
V
Laboratoire d'Electrochimie Moléculaire, UMR CNRS 7591, Université Paris Diderot, 2 place Jussieu, Paris Cedex 05, France. veronique.balland@univ-paris-diderot.fr
Hureau
Christelle
C
Cusano
Angela Maria
AM
Liu
Yingli
Y
Tron
Thierry
T
Limoges
Benoît
B
D001483:Base Sequence; D017931:DNA Primers; D004566:Electrodes; D006639:Histidine / Q000737:chemistry*; D042845:Laccase / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry
D017931:DNA Primers; D011994:Recombinant Proteins; D006639:Histidine; D042845:Laccase