Inelastic Electron Tunneling Spectroscopic Analysis of Bias-Induced Structural Changes in a Solid-State Protein Junction

A central issue in protein electronics is how far the structural stability of the protein is preserved under the very high electrical field that it will experience once a bias voltage is applied. This question is studied on the redox protein Azurin in the solid-state Au/protein/Au junction by monitoring protein vibrations during current transport under applied bias, up to approximate to 1 GV m(-1), by electrical detection of inelastic electron transport effects. Characteristic vibrational modes, such as C-H stretching, amide (N-H) bending, and Au-S (of the bonds that connect the protein to an Au electrode), are not found to change noticeably up to 1.0 V. At >1.0 V, the N-H bending and C-H stretching inelastic features have disappeared, while the Au-S features persist till approximate to 2 V, i.e., the proteins remain Au bound. Three possible causes for the disappearance of the N-H and C-H inelastic features at high bias, namely, i) resonance transport, ii) metallic filament formation, and iii) bond rupture leading to structural changes in the protein are proposed and tested. The results support the last option and indicate that spectrally resolved inelastic features can serve to monitor in operando structural stability of biological macromolecules while they serve as electronic current conduit.

Automated summary

This study investigates the structural stability of proteins under high electrical fields in a Au/protein/Au junction. The results show that the protein's vibrational modes remain largely unchanged up to 1.0 V, but certain features disappear at higher bias voltages. The disappearance of these features is likely due to bond rupture in the protein, indicating that inelastic features can be used to monitor the structural stability of biological macromolecules under high electrical fields.