Laccases (E.C. 184.108.40.206) are multicopper oxidases catalytically active in the oxidation of diphenolics and related compounds by molecular dioxygen. The laccases contain a single-copper type I center and a trinuclear cluster of a single-copper type II and a dinuclear type III center. The oxidation of four equivalents of substrate near the type I copper and the sequential transfer of electrons to the trinuclear cluster are coupled with four-electron reduction of O2 to H2O at the latter site. Extensive efforts have been given to kinetic and structural characterization of numerous laccases to elucidate the catalytic mechanism, where laccase (sub)monolayer voltammetry has been a core approach. In this report, we address voltammetry and electrocatalysis of O2 reduction of (sub)monolayers of several laccases in new ways. These are based on the use of single-crystal, atomically planar bare Au(111)-electrode surfaces or surfaces modified by thiol-based self-assembled molecular monolayers. These well-defined surfaces enable introducing electrochemical scanning tunneling microscopy directly in aqueous biological media in which the enzymes are operative (in situ STM), to the level of resolution of the single enzyme molecule in electrocatalytic action. Enzyme-electrode electronic contact and intramolecular electron transfer triggered by the electrode potential or by O2-substrate binding to the enzyme, followed at the single-molecule level, are the most important observations of this study. © 2011 American Chemical Society.
|Journal||Journal of Physical Chemistry Part C: Nanomaterials and Interfaces|
|Publication status||Published - 2012|
- Enzyme electrodes
- Scanning tunneling microscopy
- Self assembled monolayers
- Single crystal surfaces