| Popis: |
Electron transfer (ET) through proteins, a fundamental element of many biochemical reactions, has been studied intensively in solution. We report the results of electron transport (ETp) measurements across proteins, sandwiched between two solid electrodes with a long-range goal of understanding in how far protein properties are expressed (and can be utilized) in such a configuration. While most such studies to date were conducted with one or just a few molecules in the junction, we present the high yield, reproducible preparation of large area monolayer junctions of proteins from three different families: Azurin (Az), a blue-copper ET protein, Bacteriorhodopsin (bR), a membrane protein-chromophore complex with a proton pumping function, and Bovine Serum Albumin (BSA). Surprisingly, the current-voltage (I-V) measurements on such junctions, which are highly reproducible, show relatively minor differences between Az and bR, even though the latter lacks a known ET function. ETp across both Az and bR is much more efficient than across BSA, but also for the latter the currents are still high, and the decay coefficients too low to be consistent with coherent tunneling. Rather, inelastic hopping is proposed to dominate ETp in these junctions. Other features such as asymmetrical I-V curves and distinct behavior of different proteins can be viewed as molecular signatures in the solid-state conductance. |
