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Oriented Immobilization of a Fully Active Monolayer of Histidine‐Tagged Recombinant Laccase on Modified Gold Electrodes
Author(s) -
Balland Véronique,
Hureau Christelle,
Cusano Angela Maria,
Liu Yingli,
Tron Thierry,
Limoges Benoît
Publication year - 2008
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.200800368
Subject(s) - laccase , monolayer , histidine , chemistry , cyclic voltammetry , combinatorial chemistry , redox , linker , biosensor , electrode , immobilized enzyme , active site , self assembled monolayer , enzyme , electrochemistry , inorganic chemistry , organic chemistry , biochemistry , computer science , operating system
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.