Interfacial electrochemical electron transfer (ET) of redox metalloproteins is long established. For the proteins to retain full ET or enzyme activity, modification of the electrode surfaces, such as goldsurfaces by self-assembled molecular monolayers (SAMs), is nearly always required, where pure and functionalized alkanethiols have emerged as core linkers. We overview first binding and single-molecule long-range electron transfer of some metalloproteins, metalloenzymes, and DNA-based molecules on single-crystal Au(111), Au(100), and Au(100) electrode surfaces, bound either directly by Au-S linking of surface cysteines to the gold surfaces, or indirectly by non-covalent linking to SAMs of pure and functionalized alkanethiols. Core techniques are electrochemistry, surface spectroscopies, and in situ STM and AFM under electrochemical potential control, framed by single-molecule charge transport theory and electronic structure computations. Molecular packing, voltammetry and in situ STM/AFM are found to be exceedingly sensitive to the structure of the thiol-based SAM molecules, testifying both to the crucial importance of the Au-S binding, and to the SAM linking to the protein. A primary focus that has emerged is the electronic structure of the Au-S link and the packing of the SAMs. We have, first disentangled a wealth of data to identify the nature of the core Au-S contact. All data suggest that the electronic Au-S link is dominated by a Au(0)-thiyl radical with strong vander Waals forces and not by a Au(I)-thiolate ionic/covalent unit. Molecular packing is, further crucially determined by the SAM molecular structure and involves binding either to Au-atoms mined out of the surface or directly to a flat single-crystal surface. We illustrate this by high-resolution in situ STM of straight, branched, and chiral alkanethiols on Au(111)-electrode surfaces.
|Conference||2nd Gerischer-Kolb Symposium|
|Period||11/10/2017 → 13/10/2017|