Ubiquitous Electron Transport in Non-Electron Transfer Proteins.

Many proteins that have no known role in electron transfer processes are excellent electronic conductors. This surprising characteristic is not generally evident in bulk aggregates or crystals, or in isolated, solvated peptides, because the outer hydrophilic shell of the protein presents a barrier to charge injection. Ligands that penetrate this barrier make excellent electrical contacts, yielding conductivities on the order of a S/m. The Fermi Energy of metal electrodes is aligned with the energy of internal electronic states of the protein, as evidenced by resonant transmission peaks at about 0.3V on the Normal Hydrogen Electrode scale. This energy is about 0.7 V less than the oxidation potential of aromatic amino acids, indicating a large reduction in electrostatic reorganization energy losses in the interior of the proteins. Consistent with a possible biological role for this conductance, there is a strong dependence on protein conformation. Thus, direct measurement of conductance is a powerful new way to read out protein conformation in real time, opening the way to new types of single molecule sensors and sequencing devices.