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Related Concept Videos

Electron Transport Chains01:28

Electron Transport Chains

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The final stage of cellular respiration is oxidative phosphorylation that consists of two steps: the electron transport chain and chemiosmosis. The electron transport chain is a set of proteins found in the inner mitochondrial membrane in eukaryotic cells. Its primary function is to establish a proton gradient that can be used during chemiosmosis to produce ATP and generate electron carriers, such as NAD+ and FAD, that are used in glycolysis and the citric acid cycle.
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The electron transport chain or oxidative phosphorylation is an exothermic process in which free energy released during electron transfer reactions is coupled to ATP synthesis. This process is a significant source of energy in aerobic cells, and therefore inhibitors of the electron transport chain can be detrimental to the cell's metabolic processes.
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The light reactions of photosynthesis assume a linear flow of electrons from water to NADP+. During this process, light energy drives the splitting of water molecules to produce oxygen. However, oxidation of water molecules is a thermodynamically unfavorable reaction and requires a strong oxidizing agent. This is accomplished by the first product of light reactions: oxidized P680 (or P680+), the most powerful oxidizing agent known in biology. The oxidized P680 that acquires an electron from the...
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The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
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Electron Transport Chain Components01:29

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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...
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Updated: Feb 11, 2026

All-electronic Nanosecond-resolved Scanning Tunneling Microscopy: Facilitating the Investigation of Single Dopant Charge Dynamics
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Tunneling explains efficient electron transport via protein junctions.

Jerry A Fereiro1, Xi Yu2, Israel Pecht3

  • 1Department of Materials and Interfaces, Weizmann Institute of Science, Rehovot 7610001, Israel.

Proceedings of the National Academy of Sciences of the United States of America
|May 2, 2018
PubMed
Summary

Electron transport in metalloproteins like azurin (Az) can be dominated by quantum tunneling. Researchers observed a switch between off-resonant and resonant tunneling by altering protein-electrode coupling, revealing the metal ion

Keywords:
bioelectronicsprotein IETSprotein junctionsresonance tunnelingtemperature dependence

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Area of Science:

  • Biophysics
  • Molecular Electronics
  • Quantum Chemistry

Background:

  • Metalloproteins are crucial electron transfer agents in biological systems.
  • Their potential use in bioelectronic devices is an active area of research.
  • Understanding electron transport mechanisms in these proteins is key for device applications.

Purpose of the Study:

  • To investigate electron transport mechanisms in protein-based monolayer junctions.
  • To explore the role of protein-electrode coupling on charge transport.
  • To identify quantum mechanical effects governing electron transport in metalloproteins.

Main Methods:

  • Low-temperature (10 K) electron transport measurements.
  • Utilized monolayer junctions based on the blue copper protein azurin (Az).
  • Varied protein-electrode coupling using molecular spacers.

Main Results:

  • Observed quantum tunneling as the dominant charge transport mechanism.
  • Demonstrated a switch from off-resonant to resonant tunneling by weakening protein-electrode coupling.
  • Identified vibronic features of the copper ion's coordination sphere influencing resonance tunneling.

Conclusions:

  • Quantum mechanical effects, specifically tunneling, play a dominant role in electron transport through protein junctions.
  • Protein-electrode coupling strength significantly influences the tunneling regime.
  • Metal ions within proteins actively participate in resonance tunneling phenomena.