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Related Concept Videos

Electron Transport Chain Components01:29

Electron Transport Chain Components

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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...
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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 I and II01:46

Electron Transport Chain: Complex I and II

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

Electron Transport Chain: Complex III and IV

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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...
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Inorganic Nitrogen Assimilation01:22

Inorganic Nitrogen Assimilation

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Nitrogen is an essential element in biological systems, forming a crucial component of proteins, nucleic acids, and other cellular constituents. Many bacteria and archaea acquire nitrogen in the form of nitrate (NO₃⁻) or ammonia (NH₃), which are then assimilated into biomolecules through specific enzymatic pathways.Assimilatory Nitrate ReductionWhen nitrate enters the cell, it undergoes a two-step reduction process known as assimilatory nitrate reduction. Initially, the enzyme...
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The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

3.1K
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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Related Experiment Video

Updated: Mar 7, 2026

Analyzing Supercomplexes of the Mitochondrial Electron Transport Chain with Native Electrophoresis, In-gel Assays, and Electroelution
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Modular electron-transport chains from eukaryotic organelles function to support nitrogenase activity.

Jianguo Yang1, Xiaqing Xie1, Mingxuan Yang1

  • 1State Key Laboratory of Protein and Plant Gene Research, College of Life Sciences, Peking University, Beijing 100871, China.

Proceedings of the National Academy of Sciences of the United States of America
|February 15, 2017
PubMed
Summary

Researchers engineered biological nitrogen fixation (BNF) in E. coli by integrating plant electron-transport components (ETCs). Chloroplast and root plastid ETCs successfully powered nitrogenase, paving the way for cereal crop diazotrophy.

Keywords:
electron transportnitrogen fixationnitrogenase engineeringplant organelles

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Plant Science

Background:

  • Biological nitrogen fixation (BNF) is crucial for plant growth but requires complex genetic machinery and is oxygen-sensitive.
  • Engineering BNF into cereal crops faces challenges due to gene complexity, energy demands, and nitrogenase's oxygen sensitivity.
  • Nitrogenase genes form three modules: electron-transport components (ETCs), metal cluster biosynthesis, and the core nitrogenase apoenzyme.

Purpose of the Study:

  • To investigate the compatibility of plant organelle ETCs with molybdenum and iron-only nitrogenases.
  • To assess the potential of using plant organelle ETCs as power sources for nitrogenase activity in a bacterial chassis.
  • To identify suitable ETCs for engineering diazotrophy in cereal crops.

Main Methods:

  • Used *Escherichia coli* as a chassis to test nitrogenase activity with plant-derived ETCs.
  • Replaced bacterial ETCs with ferredoxin-NADPH oxidoreductase (FNR) and ferredoxin genes from chloroplasts, root plastids, and mitochondria.
  • Constructed hybrid ETC modules using mitochondrial components and *Anabaena* ferredoxins to overcome incompatibilities.

Main Results:

  • The FNR-ferredoxin ETC modules from chloroplasts and root plastids effectively supported both molybdenum and iron-only nitrogenase activities.
  • Mitochondrial ETC modules were incompatible with nitrogenase electron transfer.
  • Hybrid ETC modules, combining mitochondrial oxidoreductase with specific *Anabaena* ferredoxins, restored nitrogenase function.

Conclusions:

  • Endogenous electron-transport components from plant chloroplasts and root plastids can power nitrogenase enzymes.
  • Mitochondrial ETCs require modification for nitrogenase compatibility, suggesting specific protein interactions are key.
  • This study identifies viable plant-derived power sources for nitrogenase, advancing efforts to engineer cereal crops for biological nitrogen fixation.