查看文章

Cerrena unicolor laccase was immobilized on the gold electrode by covalent bonding to self-assembled monolayers of mercaptoundecanoic or mercaptopropionic acids. STM images of immobilized laccase proved high population of the laccase molecules on the monolayer modified electrode. The SERS experiments in concert with resonance Raman effect confirmed that the structure at the “blue” copper site of the immobilized protein remained intact. The accessibility of individual copper sites for electron exchange with the gold electrode surface was investigated by voltammetry. The electrode behavior of laccase is different in the presence and absence of oxygen, showing that the immobilized enzyme is reactive towards oxygen. Addition of two common mediators improved the electrical connectivity of the enzyme with the electrode, increased the catalytic efficiency of immobilized laccase and switched the onset of …