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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: 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...

Pyruvate Oxidation

Pyruvate Oxidation

After glycolysis, the charged pyruvate molecules enter the mitochondria via active transport and undergo three enzymatic reactions. These reactions ensure that pyruvate can enter the next metabolic pathway so that energy stored in the pyruvate molecules can be harnessed by the cells.
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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...

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.
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The Electron Transport Chain

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

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Related Experiment Video

Updated: May 12, 2026

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases

Published on: February 24, 2018

Oxidative modifications of mitochondria complex II.

Liwen Zhang¹, Patrick T Kang, Chwen-Lih Chen

¹Proteomics and Mass Spectrometry Facility, Campus Chemical Instrument Center, The Ohio State University, Columbus, OH, USA.

Methods in Molecular Biology (Clifton, N.J.)

|April 23, 2013

Summary

Mitochondrial dysfunction in heart attacks involves oxidative damage to Complex II. This study details methods to identify specific oxidative modifications, aiding understanding of heart injury mechanisms.

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

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Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases

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Published on: February 24, 2018

Visualization of Mitochondrial Respiratory Function using Cytochrome C Oxidase / Succinate Dehydrogenase (COX/SDH) Double-labeling Histochemistry

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

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

Published on: July 20, 2022

Area of Science:

Biochemistry
Cardiovascular Biology
Mitochondrial Biology

Background:

Mitochondrial dysfunction, driven by superoxide (O2·−) and nitric oxide (NO), is central to myocardial ischemia/reperfusion injury.
Oxidative impairment in Complex II involves decreased S-glutathionylation and increased tyrosine nitration of its 70 kDa subunit in post-ischemic hearts.

Purpose of the Study:

To investigate Reactive Oxygen Species (ROS)-mediated oxidative modifications in Complex II relevant to myocardial infarction.
To describe a protocol for characterizing specific oxidative modifications at the Complex II 70 kDa subunit.

Main Methods:

In vitro oxidative modification of isolated Complex II using GSSG and OONO−.
Nano-liquid chromatography/tandem mass spectrometry (nano-LC/MS/MS) for detailed analysis of modified subunits.
Immunofluorescence microscopy using specific antibodies to detect protein nitration and S-glutathionylation in myocytes under oxidative stress.

Main Results:

Established a protocol for identifying specific oxidative modifications on the Complex II 70 kDa subunit.
Demonstrated the feasibility of detecting cellular oxidative modifications, including protein nitration and S-glutathionylation, using immunofluorescence microscopy.

Conclusions:

The described methods enable precise characterization of oxidative damage to Complex II.
These techniques are valuable for studying ROS-mediated mechanisms in myocardial infarction and related conditions.