Related Experiment Video
Updated: Dec 26, 2025
![Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase](/_next/image?url=https%3A%2F%2Fcloudfront.jove.com%2FCDNSource%2Fteasers%2F55858.jpg&w=3840&q=50)
10:01
Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
Published on: December 4, 2017
12.6K
Electronic Conductance Resonance in Non-Redox-Active Proteins
Bintian Zhang1, Weisi Song1, Jesse Brown2
1Biodesign Institute, Arizona State University, Tempe, Arizona 87287, United States.
Journal of the American Chemical Society
|March 17, 2020
Summary
Researchers studied non-redox-active proteins, finding they conduct electricity. A conductance resonance was observed, suggesting a new mechanism for long-range charge transport in these biological molecules.
Area of Science:
- Bioelectronics
- Molecular Biophysics
- Protein Conduction
Background:
- Bioelectronics research traditionally focuses on redox-active proteins for biological charge transport.
- Electronic conductance in redox proteins peaks at their specific redox potential.
- Recent findings indicate non-redox-active proteins also exhibit significant electronic conductivity, but the mechanism remains unclear.
Purpose of the Study:
- To investigate the mechanism of electronic conduction in non-redox-active proteins.
- To measure single-molecule conductance of non-redox-active proteins under controlled electron injection.
- To understand the factors governing charge transport in proteins lacking redox activity.
Main Methods:
- Single-molecule conductance measurements.
- Potentiostatic control of proteins in solution.
- Varying electron injection energy to probe conductance characteristics.
Main Results:
- Three non-redox-active proteins were measured.
- A consistent conductance resonance was observed for all tested proteins.
- This resonance occurred at an electron injection potential approximately 0.7 V shifted from the nearest amino acid oxidation potential.
Conclusions:
- The observed conductance resonance suggests a novel charge transport mechanism in non-redox-active proteins.
- The potential shift may indicate reduced reorganization energy within the protein interior.
- This finding could explain long-range conductance in proteins when charge carriers are injected internally.
Related Concept Videos
Redox Equilibria: Overview
1.5K
A reduction-oxidation reaction is commonly called a redox reaction. In a redox reaction, electrons are transferred from one species to another rather than being shared between or among atoms. The reducing agent or reductant is the species that loses electrons and gets oxidized in the process. The species that gains electrons and gets reduced in the process is the oxidizing agent or oxidant. Redox reactions are represented as two separate equations called half-reactions, where one equation...
1.5K
Redox Reactions
766
Redox reactions are vital biochemical processes that underpin energy metabolism in cells. These reactions involve the transfer of electrons between molecules, occurring in tandem as oxidation and reduction. Oxidation refers to the loss of electrons, while reduction denotes their gain. This coupling ensures the seamless flow of electrons through metabolic pathways. For example, in bacterial metabolism, glucose undergoes oxidation to carbon dioxide, while oxygen is simultaneously reduced to...
766
Protein Dynamics in Living Cells
2.6K
Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
2.6K
Electron Paramagnetic Resonance (EPR) Spectroscopy: Organic Radicals
3.2K
Ideally, an unpaired electron shows a single peak in the EPR spectrum due to the transition between the two spin energy states. However, coupling interactions can occur between the spins of the unpaired electron and any neighboring spin-active nuclei. This hyperfine coupling results in hyperfine splitting, where the EPR signal is split into multiplets. The signals split into 2nI + 1 peaks, where n is the number of equivalent nuclei and I is the nuclear spin. These splitting patterns provide...
3.2K
Electron Transport Chain Components
769
The electron transport chain (ETC) is a crucial metabolic pathway that facilitates energy conversion in prokaryotic and eukaryotic cells. In eukaryotes, the ETC comprises four membrane-associated protein complexes in the inner mitochondrial membrane. In prokaryotes, the ETC in the plasma membrane can vary in composition, with fewer or different complexes depending on the organism and environmental conditions. These complexes transfer electrons from electron donors, such as NADH and FADH2, to...
769

