ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2015
Electron Transfer Proteins as Electronic Conductors: Significance of the Metal and Its Binding Site in the Blue Cu Protein, Azurin.
Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Single-Molecule Conductance of Non-Redox Proteins: Mechanisms, Measurements, and Applications.Biomolecules · 2026Review
- Azurin: A Model to Study a Metal Coordination Sphere or Electron Transfer in Metalloproteins.International journal of molecular sciences · 2025Review
- Structural Gating Enhances Long-Distance Light-Driven Interfacial Electron Transfer.ACS central science · 2024Article
- Temperature-Dependent Characterization of Long-Range Conduction in Conductive Protein Fibers of Cable Bacteria.ACS nano · 2024Article
- Conductance Channels in a Single-Entity Enzyme.The journal of physical chemistry letters · 2024Article
- Electron transport through two interacting channels in Azurin-based solid-state junctions.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Efficient Electron Hopping Transport through Azurin-Based Junctions.The journal of physical chemistry letters · 2023Article
- Electron Tunneling in Biology: When Does it Matter?ACS omega · 2023Article
- Biotin Binding Hardly Affects Electron Transport Efficiency across Streptavidin Solid-State Junctions.Langmuir : the ACS journal of surfaces and colloids · 2023Article
- Role of Order in the Mechanism of Charge Transport across Single-Stranded and Double-Stranded DNA Monolayers in Tunnel Junctions.Journal of the American Chemical Society · 2021Article
- Protein Binding and Orientation Matter: Bias-Induced Conductance Switching in a Mutated Azurin Junction.Journal of the American Chemical Society · 2020Article
- Tunneling explains efficient electron transport via protein junctions.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Electron Transfer Proteins as Electronic Conductors: Significance of the Metal and Its Binding Site in the Blue Cu Protein, Azurin.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2015Article
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6 authors.
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Abstract
Electron transfer (ET) proteins are biomolecules with specific functions, selected by evolution. As such they are attractive candidates for use in potential bioelectronic devices. The blue copper protein azurin (Az) is one of the most-studied ET proteins. Traditional spectroscopic, electrochemical, and kinetic methods employed for studying ET to/from the protein's Cu ion have been complemented more recently by studies of electrical conduction through a monolayer of Az in the solid-state, sandwiched between electrodes. As the latter type of measurement does not require involvement of a redox process, it also allows monitoring electronic transport (ETp) via redox-inactive Az-derivatives. Here, results of macroscopic ETp via redox-active and -inactive Az derivatives, i.e., Cu(II) and Cu(I)-Az, apo-Az, Co(II)-Az, Ni(II)-Az, and Zn(II)-Az are reported and compared. It is found that earlier reported temperature independence of ETp via Cu(II)-Az (from 20 K until denaturation) is unique, as ETp via all other derivatives is thermally activated at temperatures >≈200 K. Conduction via Cu(I)-Az shows unexpected temperature dependence >≈200 K, with currents decreasing at positive and increasing at negative bias. Taking all the data together we find a clear compensation effect of Az conduction around the Az denaturation temperature. This compensation can be understood by viewing the Az binding site as an electron trap, unless occupied by Cu(II), as in the native protein, with conduction of the native protein setting the upper transport efficiency limit.
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