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Related Concept Videos

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.
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Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
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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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Proteins targeted to the inner chloroplast membrane, or plastid proteins, are transported by two general pathways: the stop-transfer and the re-insertion or post-import pathways. Most plastid proteins carry N-terminal transit sequences and internal import sequences targeting it to the specific chloroplast subcompartment. Proteins targeted by the stop-transfer pathway have internal hydrophobic sequences that inhibit their translocation into the stroma. As a result, these precursors are arrested...
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Protein Transport into the Inner Mitochondrial Membrane01:34

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Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Updated: Feb 7, 2026

Analyzing Supercomplexes of the Mitochondrial Electron Transport Chain with Native Electrophoresis, In-gel Assays, and Electroelution
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Transient protein structure guides surface diffusion pathways for electron transport in membrane supercomplexes.

Chun Kit Chan1, Jonathan Nguyen1, Corey F Hryc2

  • 1School of Molecular Sciences, Biodesign Institute, Arizona State University, Tempe, AZ, USA.

Nature Communications
|February 5, 2026
PubMed
Summary
This summary is machine-generated.

Mitochondrial supercomplexes guide redox proteins using disordered hinges, enhancing energy conversion efficiency by 30%. This refolding-guided diffusion mechanism optimizes electron transfer across membranes.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • The precise function of mitochondrial supercomplexes in guiding redox proteins during energy conversion is not fully understood.
  • Mitochondrial supercomplexes, particularly those involving complexes III and IV (CIII and CIV), play a crucial role in cellular respiration.

Purpose of the Study:

  • To investigate the role of mitochondrial supercomplexes, specifically CIII2CIV2, in facilitating electron transfer.
  • To elucidate the mechanism by which disordered regions within supercomplexes influence redox protein dynamics and membrane transfer.

Main Methods:

  • Integration of multiscale modeling with single particle cryo-electron microscopy (cryo-EM).
  • Utilized bioinformatic and entropy-based methods to generate structural ensembles of the yeast CIII2CIV2 supercomplex.
  • Employed Molecular Dynamics and Brownian Dynamics simulations to analyze protein-lipid interactions and diffusion.

Main Results:

  • Disordered hinge regions in CIII, specifically QCR6, electrostatically couple with redox proteins, promoting their binding and directional diffusion across the membrane.
  • The inherent disorder in the hinge region lowers the diffusion barrier for electron transfer, rather than impeding it.
  • Anionic lipids were found to enhance this process by maintaining a membrane pool of redox proteins, crucial for efficient transfer.
  • Cryo-EM analysis of supercomplexes lacking QCR6 (ΔQCR6) revealed rearrangements but maintained surface-mediated transfer capabilities.

Conclusions:

  • Mitochondrial supercomplexes utilize a refolding-guided diffusion mechanism for electron carriers confined on bioenergetic membranes.
  • This mechanism significantly enhances supercomplex energy conversion efficiency by approximately 30%.
  • The study provides new insights into the dynamic structural roles of mitochondrial supercomplexes in bioenergetics.