Electron transport through two interacting channels in Azurin-based solid-state junctions.

ABSTRACT: The fundamental question of "what is the transport path of electrons through proteins?" initially introduced while studying long-range electron transfer between localized redox centers in proteins in vivo is also highly relevant to the transport properties of solid-state, dry metal-protein-metal junctions. Here, we report conductance measurements of such junctions, Au-(Azurin monolayer ensemble)-Bismuth (Bi) ones, with well-defined nanopore geometry and ~10³ proteins/pore. Our results can be understood as follows. (1) Transport is via two interacting conducting channels, characterized by different spatial and time scales. The slow and spatially localized channel is associated with the Cu center of Azurin and the fast delocalized one with the protein's polypeptide m

SUBMITTER: Li P 

PROVIDER: S-EPMC11331140 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature