Abstract
Various aspects of redox protein integration with nano-electronic elements are addressedby a multi-technique investigation of different yeast cytochrome c (YCC)-basedhybrid systems. Three different immobilization strategies on gold via organiclinkers are explored, involving either covalent bonding or electrostatic interaction.Specifically, Au surfaces are chemically modified by self-assembled monolayers(SAMs) exposing thiol-reactive groups, or by acid-oxidized single-wall carbonnanotubes (SWNTs). Atomic force microscopy and scanning tunnelling microscopyare employed to characterize the morphology and the electronic properties ofsingle YCC molecules adsorbed on the modified gold surfaces. In each hybridsystem, the protein molecules are stably assembled, in a native configuration.A standing-up arrangement of YCC on SAMs is suggested, together with anenhancement of the molecular conduction, as compared to YCC directly assembled ongold. The electrostatic interaction with functionalized SWNTs allows severalYCC adsorption geometries, with a preferential high-spin haem configuration, asoutlined by Raman spectroscopy. Moreover, the conduction properties of YCC,explored in different YCC nanojunctions by conductive atomic force microscopy,indicate the effectiveness of electrical conduction through the molecule and itsdependence on the electrode material. The joint employment of several techniquesconfirms the key role of a well-designed immobilization strategy, for optimizingbiorecognition capabilities and electrical coupling with conductive substrates at thesingle-molecule level, as a starting point for advanced applications in nano-biotechnology.
Published Version
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