Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Electron Transport Chain: Complex III and IV01:43

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 Chains01:28

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 Components01:29

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...
Electron Transport Chain: Complex I and II01:46

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...
The Electron Transport Chain01:30

The Electron Transport Chain

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.
Inhibitors of the electron transport chain
Rotenone, a widely used pesticide, prevents electron transfer from Fe-S cluster to ubiquinone or Q in...
Chemiosmosis and ATP Synthesis01:22

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...

You might also read

Related Articles

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

Sort by
Same author

Structural insights into a conserved mechanism of choline translocation through CHT.

Science advances·2026
Same author

<i>In Silico</i> Optimization of a Bifunctional Lipase-Polyethylene Terephthalate (PET) Hydrolase for Enhanced PET and Lipid Hydrolysis.

Journal of chemical information and modeling·2026
Same author

Molecular Insights into the Activation of a Fungal Copper Radical Oxidase by Peroxidases.

Chem & bio engineering·2026
Same author

A la carte bioprospecting of substrate-selective laccases via high-throughput computational enzyme-substrate interaction profiling.

Protein science : a publication of the Protein Society·2026
Same author

Engineering <i>Escherichia coli</i> for polyethylene terephthalate powder biodegradation via recoding of an outer membrane protein.

iScience·2026
Same author

Unraveling the impact of cyclic peptide primary structure on rotaxane formation through umbrella sampling molecular dynamics simulations.

Physical chemistry chemical physics : PCCP·2026

Related Experiment Video

Updated: Jun 3, 2026

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
10:01

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

Published on: December 4, 2017

Electron transfer pathways in cytochrome c oxidase.

M Fátima Lucas1, Denis L Rousseau, Victor Guallar

  • 1Barcelona Supercomputing Center, Jordi Girona, Barcelona, Spain.

Biochimica Et Biophysica Acta
|March 23, 2011
PubMed
Summary

Cytochrome c oxidase

Area of Science:

  • Biochemistry
  • Computational Chemistry
  • Enzyme Mechanisms

Background:

  • Cytochrome c oxidase is a key enzyme in cellular respiration, catalyzing oxygen reduction to water.
  • Understanding its electron transfer pathway is crucial for comprehending energy production.
  • Previous studies have implicated specific redox centers and residues, but the precise pathway remains under investigation.

Purpose of the Study:

  • To elucidate the electron transfer pathway in cytochrome c oxidase using computational methods.
  • To identify key residues and their roles in facilitating electron transfer.
  • To investigate the influence of positive charges and proton-coupled electron transfer.

Main Methods:

  • Mixed quantum mechanical/molecular mechanics (QM/MM) calculations were employed.

More Related Videos

Measuring Trans-Plasma Membrane Electron Transport by C2C12 Myotubes
10:27

Measuring Trans-Plasma Membrane Electron Transport by C2C12 Myotubes

Published on: May 4, 2018

High-Resolution Respirometry to Assess Bioenergetics in Cells and Tissues Using Chamber- and Plate-Based Respirometers
09:53

High-Resolution Respirometry to Assess Bioenergetics in Cells and Tissues Using Chamber- and Plate-Based Respirometers

Published on: October 26, 2021

Related Experiment Videos

Last Updated: Jun 3, 2026

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
10:01

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

Published on: December 4, 2017

Measuring Trans-Plasma Membrane Electron Transport by C2C12 Myotubes
10:27

Measuring Trans-Plasma Membrane Electron Transport by C2C12 Myotubes

Published on: May 4, 2018

High-Resolution Respirometry to Assess Bioenergetics in Cells and Tissues Using Chamber- and Plate-Based Respirometers
09:53

High-Resolution Respirometry to Assess Bioenergetics in Cells and Tissues Using Chamber- and Plate-Based Respirometers

Published on: October 26, 2021

  • Density functional calculations were performed on the enzyme's redox centers (Cu(A), heme a, heme a(3)).
  • The QM/MM e-pathway method was utilized to map electron transfer routes and identify critical residues.

    • Main Results:

    • The electron transfer sequence was characterized as Cu(A)→heme a→heme a(3).
    • Positive charges significantly influence the electron transfer process, supporting proton-coupled electron transfer.
    • Key residues, particularly arginines 481 and 482, were identified as crucial for electron transfer between redox centers.

    Conclusions:

    • The study provides a detailed map of the electron transfer pathway in cytochrome c oxidase.
    • Arginine residues 481 and 482 play a vital role in facilitating electron transfer.
    • Computational QM/MM e-pathway analysis offers valuable insights into enzyme mechanisms and is consistent with experimental findings.