Abstract
We studied the coherent electron transport through metal–protein–metal junctions based on a blue copper azurin, in which the copper ion was replaced by three different metal ions (Co, Ni and Zn). Our results show that neither the protein structure nor the transmission at the Fermi level change significantly upon metal replacement. The discrepancy with previous experimental observations suggests that the transport mechanism taking place in these types of junctions is probably not fully coherent.
Highlights
The study of metal–protein–metal junctions has opened up new avenues in the field of molecular electronics as it paves the way to develop new hybrid devices capable of exploiting proteins’ remarkable properties [1]
We refer to X-azurin (X = Ni, Cu, Co and Zn) as the azurin containing the X-ion
From the structure overlap between the different proteins and native azurin (i.e., Cu-azurin), it becomes apparent that the ion replacement has little influence on the protein conformation
Summary
The study of metal–protein–metal junctions has opened up new avenues in the field of molecular electronics as it paves the way to develop new hybrid devices capable of exploiting proteins’ remarkable properties [1] They have the inherent capability of transferring charge over long distances. The significant amount of work accumulated in recent years on this topic has given rise to a new field, namely that of protein-based electronics, which has been given the name of proteotronics [7]. Research in this field has been carried out on various fronts. Research on the transport properties of the building blocks of proteins, namely amino acids and peptides, has been carried out [12,13,14]
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