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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 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...

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...

ATP Synthase: Mechanism

ATP Synthase: Mechanism

In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased ATP...

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...

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Related Experiment Video

Updated: Jul 12, 2026

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Published on: September 14, 2014

Electron-tunneling pathways in cytochrome C.

D S Wuttke, M J Bjerrum, J R Winkler

Science (New York, N.Y.)

|May 15, 1992

Summary

Electronic couplings between iron and ruthenium in cytochrome c derivatives were measured. These couplings correlate with electron transfer pathway lengths, not just distance, with through-space jumps significantly reducing coupling strength.

Area of Science:

Biochemistry
Physical Chemistry
Molecular Biophysics

Background:

Cytochrome c is a crucial protein in electron transport.
Understanding electron transfer mechanisms is vital for biological processes.
Histidine residues play a key role in coordinating metal ions and mediating electron transfer.

Purpose of the Study:

To quantify distant electronic couplings between Fe(2+) and Ru(3+) in modified cytochrome c.
To investigate the relationship between electronic couplings, pathway length, and distance.
To elucidate the impact of through-space jumps on electron transfer pathways.

Main Methods:

Intramolecular electron transfer rate measurements in Ru(histidine(x)) cytochrome c derivatives.
Analysis of electronic couplings based on experimental rates.

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

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Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

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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

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Correlation of couplings with histidine-heme distances and sigma-tunneling pathway lengths.

Main Results:

Electronic couplings were successfully extracted and quantified for four cytochrome c derivatives.
The order of couplings did not align with simple histidine-heme edge-edge distances.
Couplings correlated with the length of sigma-tunneling pathways, including covalent bonds, hydrogen bonds, and through-space jumps.
A specific through-space jump (Pro71 to Met80) significantly increased the pathway length and decreased coupling for His72.

Conclusions:

Electron transfer couplings are sensitive to the detailed structure of the tunneling pathway, not solely the distance.
Through-space jumps represent significant barriers that reduce electronic coupling strength.
This study provides insights into the factors governing long-range electron transfer in metalloproteins.