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Related Concept Videos

Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

9.7K
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...
9.7K
Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

19.5K
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...
19.5K
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.
The ETC is comprised of...
116.2K
Oxidation of Phenols to Quinones01:17

Oxidation of Phenols to Quinones

5.2K
In the presence of oxidizing agents, phenols are oxidized to quinones. Quinones can be easily reduced back to phenols using mild reducing agents. The electron-donating hydroxyl group enhances the reactivity of the aromatic ring, enabling oxidation of the ring even in the absence of an α hydrogen.
o-hydroxy phenols are oxidized to o-quinones and p-hydroxy phenols to p-quinones. Such redox reactions involve the transfer of two electrons and two protons. The reversible redox...
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The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

3.2K
The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
3.2K
The Electron Transport Chain01:30

The Electron Transport Chain

21.4K
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...
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Related Experiment Video

Updated: Mar 26, 2026

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
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Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools

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Understanding Ubiquinone.

Ying Wang1, Siegfried Hekimi1

  • 1Department of Biology, McGill University, Montreal, QC, H3A 1B1, Canada.

Trends in Cell Biology
|February 1, 2016
PubMed
Summary

Ubiquinone (coenzyme Q) plays a dual role in mitochondria, acting as both a pro-oxidant and antioxidant. New mouse models reveal its complex functions impacting aging and disease, questioning its therapeutic potential.

Area of Science:

  • Mitochondrial biology
  • Oxidative stress research
  • Aging and disease mechanisms

Background:

  • Ubiquinone (coenzyme Q) is a key mitochondrial electron transport chain component.
  • Its dual role as a pro-oxidant and antioxidant is central to aging and disease debates.
  • Understanding ubiquinone's function is critical for addressing mitochondrial dysfunction.

Purpose of the Study:

  • To investigate the precise roles and requirements of ubiquinone in various cellular contexts.
  • To elucidate the impact of ubiquinone on mitochondrial function and reactive oxygen species (ROS) production.
  • To re-evaluate ubiquinone's therapeutic potential in aging and disease.

Main Methods:

  • Utilized novel transgenic mouse models.
  • Analyzed ubiquinone's function across different cell types and subcellular locations.
Keywords:
coenzyme Qelectron transportmitochondriareactive oxygen speciesubiquinone

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  • Investigated the interplay between ubiquinone, mitochondria, and ROS.

    • Main Results:

    • New insights into ubiquinone's necessity in specific cellular processes and locations.
    • Demonstrated unexpected functions of ubiquinone in the context of aging.
    • Challenged existing models of ubiquinone's pro-oxidant and antioxidant activities.

    Conclusions:

    • Ubiquinone's role in aging and disease is more complex than previously understood.
    • Transgenic mouse models provide critical data for dissecting ubiquinone's functions.
    • Further research is needed to clarify ubiquinone's mechanisms of action as a therapeutic agent.