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Related Concept Videos

Electron Transport Chain Components01:29

Electron Transport Chain Components

199
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...
199
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...
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Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

8.0K
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...
8.0K
Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

14.9K
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...
14.9K
The Electron Transport Chain01:30

The Electron Transport Chain

17.2K
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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The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

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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...
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Updated: Sep 6, 2025

Analyzing Supercomplexes of the Mitochondrial Electron Transport Chain with Native Electrophoresis, In-gel Assays, and Electroelution
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Characterizing the Electron Transport Chain: Structural Approach.

Ting Liang1,2, Janice Deng2, Bijaya Nayak2

  • 1Key Laboratory of Laboratory Medicine, Ministry of Education, Zhejiang Provincial Key Laboratory of Medical Genetics, College of Laboratory Medicine and Life Sciences, Wenzhou Medical University, Wenzhou, Zhejiang, China.

Methods in Molecular Biology (Clifton, N.J.)
|June 30, 2022
PubMed
Summary
This summary is machine-generated.

This study details protocols for analyzing mitochondrial respiratory chain structures, focusing on supercomplexes. These methods aid in understanding mitochondrial defects linked to human diseases.

Keywords:
AssemblyBlue Native GelBrainMuscleRespiratory complex

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Mitochondrial Biology

Background:

  • The mitochondrial respiratory chain, essential for oxidative phosphorylation (OXPHOS), comprises five multi-subunit protein complexes.
  • Respiratory chain supercomplexes, formed by multiple respiratory complexes, are increasingly recognized for their role in regulating OXPHOS function.
  • Dysfunction in the respiratory chain and its regulation is implicated in human diseases like neurodegenerative and muscular disorders.

Purpose of the Study:

  • To present detailed protocols for analyzing the structure of the mitochondrial respiratory chain, particularly its supercomplexes.
  • To provide methods for investigating mitochondrial defects in mouse models relevant to human diseases.
  • To facilitate the study of respiratory complex assembly and function.

Main Methods:

  • Tissue sample preparation from mouse models with mitochondrial defects.
  • Isolation of mitochondrial membrane proteins.
  • Analysis of respiratory complexes and supercomplexes using Blue Native Polyacrylamide Gel Electrophoresis (BN-PAGE).

Main Results:

  • Established protocols for the preparation and isolation of mitochondrial membrane proteins.
  • Demonstrated the application of BN-PAGE for analyzing the structural organization of respiratory chain complexes and supercomplexes.
  • Provided a framework for comparative analysis of mitochondrial respiratory chain structures.

Conclusions:

  • The presented protocols are crucial for dissecting the structural basis of mitochondrial respiratory chain dysfunction.
  • These methods enable detailed analysis of respiratory supercomplexes, offering insights into disease mechanisms.
  • The study provides valuable tools for researchers investigating mitochondrial disorders and OXPHOS regulation.