Protein Electronic Energy Transport Levels Derived from High-Sensitivity Near-UV and Constant Final State Yield Photoemission Spectroscopy

Proteins are attractive as functional components in molecular junctions. However, controlling the electronic charge transport via proteins, held between two electrodes, requires information on their frontier orbital energy level alignment relative to the electrodes’ Fermi level (E_F), which normally requires studies of UV Photoemission Spectroscopy (UPS) with HeI excitation. Such excitation is problematic for proteins, which can denature under standard measuring conditions. Here high-sensitivity soft UV photoemission spectroscopy (HS-UPS) combined with Constant Final State Yield Spectroscopy (CFS-YS) is used to get this information for electrode/protein contacts. Monolayers of the redox protein Azurin, (Az) and its Apo-form on Au substrates, have HOMO onset energies, obtained from CFS-YS, differ by ≈0.2 eV, showing the crucial role of the Cu redox centre in the electron transport process. It is found that combined HS-UPS/CFS-YS measurements agree with the Photoelectron Yield Spectroscopy (PYS), showing potential of the HS-UPS + CFS-YS as a powerful tool to characterize and map the energetics of a protein-electrode interfaces, which will aid optimizing design of devices with targeted electronic properties, as well as for novel applications.