Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Electron Transport Chains

Electron Transport Chains

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.
The ETC is comprised of...

Electron Transport Chain: Complex III and IV

Electron Transport Chain: Complex III and IV

During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...

Electron Transport Chain Components

Electron Transport Chain Components

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...

Chemiosmosis and ATP Synthesis

Chemiosmosis and ATP Synthesis

The electron transport chain is a critical component of cellular respiration, occurring in the inner mitochondrial membrane. It facilitates the transfer of high-energy electrons from reduced cofactors NADH and FADH₂ to molecular oxygen, the final electron acceptor. This transfer of electrons through a series of protein complexes is tightly coupled to the translocation of protons across the membrane, generating a proton gradient essential for ATP synthesis.Electron Flow and Proton...

Chemiosmosis

Chemiosmosis

Oxidative phosphorylation is a highly efficient process that generates large amounts of adenosine triphosphate (ATP), the basic unit of energy that drives many cellular processes. Oxidative phosphorylation involves two processes— the electron transport chain and chemiosmosis.
Electron Transport Chain
The electron transport chain involves a series of protein complexes on the inner mitochondrial membrane that undergo a series of redox reactions. At the end of this chain, the electrons reduce...

Electron Transport Chain: Complex I and II

Electron Transport Chain: Complex I and II

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.
ROS generation is regulated and maintained at moderate levels necessary...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Electrostatic and proton-electron interaction in membrane-bound charge transfer proteins under external electric fields: a computational study.

Physical chemistry chemical physics : PCCP·2026

Same author

Protein charge transfer far from equilibrium: a theoretical perspective.

Physical chemistry chemical physics : PCCP·2023

Same author

A trick of the tail: computing the entropic contribution to the energetics of quinone-protein unbindung.

Physical chemistry chemical physics : PCCP·2023

Same author

Water purification modeling by functionalized hourglass-shape multilayer nano-channel.

Journal of molecular graphics & modelling·2023

Same author

The Unified Redox Scale for All Solvents: Consistency and Gibbs Transfer Energies of Electrolytes from their Constituent Single Ions.

Chemistry (Weinheim an der Bergstrasse, Germany)·2023

Same author

Protonation and orientation: a computational approach to cocaine diffusion through a model membrane.

Physical chemistry chemical physics : PCCP·2022

Search research articles

Related Experiment Video

Updated: May 7, 2026

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on ¹⁵N Metabolic Labeling and Quantitative Mass Spectrometry

Published on: March 13, 2014

Charge transfer through a cytochrome multiheme chain: theory and simulation.

Fabian Burggraf¹, Thorsten Koslowski

¹Institut für Physikalische Chemie, Universität Freiburg, Albertstraße 23a, D-79104 Freiburg im Breisgau, Germany; Institut für Technische Thermodynamik, Deutsches Zentrum für Luft- und Raumfahrt (DLR), Pfaffenwaldring 38-40, D-70569 Stuttgart, Germany.

Biochimica Et Biophysica Acta

|September 24, 2013

Summary

This study investigates electron transfer in Rhodopseudomonas viridis. Findings suggest only the two nearest hemes rapidly recharge the photoreaction center, while others may store electrons.

Keywords:

Charge transfer Marcus theory Molecular dynamics Photoreaction center Rps. viridis Simulations

More Related Videos

Analyzing Supercomplexes of the Mitochondrial Electron Transport Chain with Native Electrophoresis, In-gel Assays, and Electroelution

Analyzing Supercomplexes of the Mitochondrial Electron Transport Chain with Native Electrophoresis, In-gel Assays, and Electroelution

Published on: June 1, 2017

Characterizing Electron Transport through Living Biofilms

Characterizing Electron Transport through Living Biofilms

Published on: June 1, 2018

Related Experiment Videos

Last Updated: May 7, 2026

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on ¹⁵N Metabolic Labeling and Quantitative Mass Spectrometry

Published on: March 13, 2014

Analyzing Supercomplexes of the Mitochondrial Electron Transport Chain with Native Electrophoresis, In-gel Assays, and Electroelution

Analyzing Supercomplexes of the Mitochondrial Electron Transport Chain with Native Electrophoresis, In-gel Assays, and Electroelution

Published on: June 1, 2017

Characterizing Electron Transport through Living Biofilms

Characterizing Electron Transport through Living Biofilms

Published on: June 1, 2018

Area of Science:

Biophysics
Biochemistry
Theoretical Chemistry

Background:

The c-type cytochrome subunit in Rhodopseudomonas viridis contains a chain of four heme cofactors crucial for its function.
Understanding sequential charge transfer is vital for elucidating the mechanism of the photosynthetic reaction center.

Purpose of the Study:

To theoretically investigate the sequential charge transfer dynamics within the four-heme chain of Rhodopseudomonas viridis.
To compute key Marcus theory parameters and electron transfer rates for the heme cofactors.

Main Methods:

Utilized molecular dynamics simulations with thermodynamic integration to calculate the driving force (ΔG) and reorganization energy (λ).
Estimated interheme electronic couplings using ab initio wave functions and a semiempirical scheme for long-range interactions.

Main Results:

The outer sphere contribution to reorganization energy was found to be negligible due to limited cofactor exposure.
Calculated charge transfer rates indicate that only the two hemes closest to the membrane are involved in rapid photoreaction center recharging.

Conclusions:

The two membrane-proximal hemes likely facilitate fast recharging of the photoreaction center.
The remaining hemes may function in intermediate electron storage, a hypothesis that can be experimentally tested.