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Related Concept Videos

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

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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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Protein Complexes with Interchangeable Parts01:57

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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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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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Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Related Experiment Video

Updated: Aug 23, 2025

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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Structure and functionality of a multimeric human COQ7:COQ9 complex.

Mateusz Manicki1, Halil Aydin2, Luciano A Abriata3

  • 1Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110, USA; Morgridge Institute for Research, Madison, WI 53715, USA.

Molecular Cell
|October 28, 2022
PubMed
Summary
This summary is machine-generated.

Researchers elucidated the structure of key proteins involved in Coenzyme Q (CoQ) synthesis. This discovery reveals how COQ7 and COQ9 cooperate to produce essential CoQ for cellular metabolism and antioxidant defense.

Keywords:
COQ7COQ9coenzyme Qdi-iron proteinsmitochondriaprotein-lipid complexprotein-membrane interactionquinone biosynthesis

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Last Updated: Aug 23, 2025

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

  • Biochemistry
  • Molecular Biology
  • Cellular Metabolism

Background:

  • Coenzyme Q (CoQ) is a vital redox-active lipid crucial for cellular respiration and antioxidant functions.
  • CoQ synthesis occurs on the mitochondrial inner membrane via a poorly understood enzyme complex, termed
  • complex Q
  • .

Purpose of the Study:

  • To elucidate the structure and function of the CoQ synthesis complex.
  • To understand the roles of COQ7 and COQ9 in Coenzyme Q production.

Main Methods:

  • Presented structure-function analyses of a lipid-, substrate-, and NADH-bound complex.
  • Utilized molecular dynamics simulations to model protein-membrane interactions.

Main Results:

  • Revealed that COQ7 has a ferritin-like fold with a hydrophobic channel enhanced by COQ9.
  • Demonstrated that COQ7:COQ9 heterodimers form tetramers that deform the membrane, potentially facilitating CoQ precursor translocation.
  • Observed the assembly of two tetramers into a soluble octamer capturing a pseudo-bilayer of lipids.

Conclusions:

  • COQ7 and COQ9 work together to access membrane-bound precursors.
  • The complex coordinates CoQ synthesis steps, ensuring efficient production of this essential molecule.