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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.
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The Supercomplexes in the Crista Membrane01:41

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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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The inner mitochondrial membrane is the primary site of ATP synthesis. The inner membrane domain that forms a smooth layer adjacent to the outer membrane is called the inner boundary membrane. This domain contains membrane transporters that drive metabolites in and out of the mitochondria.  In contrast, the inner membrane network that invaginates into the matrix space is called the cristae membrane. This domain accounts for principle mitochondrial function as it accommodates the protein...
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Structure of Porins01:21

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Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
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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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Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
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Related Experiment Video

Updated: Mar 26, 2026

Author Spotlight: Unveiling Oxidative Phosphorylation System Dynamics and Mitochondrial Roles in Health and Disease
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Plant mitochondrial Complex I composition and assembly: A review.

Nitya Subrahmanian1, Claire Remacle2, Patrice Paul Hamel3

  • 1The Ohio State University, Department of Molecular Genetics, 500 Aronoff Laboratory, 318 W. 12th Avenue, Columbus, OH 43210, USA.

Biochimica Et Biophysica Acta
|January 24, 2016
PubMed
Summary

Plant Complex I, crucial for ATP production, has over 40 subunits and requires assembly factors for proper function. Research in plants like Arabidopsis thaliana reveals conserved and unique subunits, with only two known plant assembly factors, GLDH and INDH.

Keywords:
Arabidopsis thalianaAssembly factorsCarbonic anhydraseChlamydomonas reinhardtiiComplex IGldhIndhMitochondria

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Area of Science:

  • Mitochondrial respiration
  • Enzyme assembly
  • Plant biochemistry

Background:

  • Oxidative phosphorylation generates ATP via multimeric enzymes in the mitochondrial inner membrane.
  • Complex I (NADH:ubiquinone oxidoreductase) is the initial, complex enzyme in this process, comprising over 40 subunits, an FMN molecule, and eight Fe-S clusters.
  • Understanding Complex I assembly is vital for comprehending cellular energy production.

Purpose of the Study:

  • To review current knowledge on plant Complex I composition and assembly.
  • To compare plant Complex I with mammalian and fungal counterparts.
  • To highlight the limited understanding of plant-specific subunits and assembly factors.

Main Methods:

  • Genetic and proteomic analyses of Complex I mutants in plant model systems (Arabidopsis thaliana, Chlamydomonas reinhardtii).
  • Comparative analysis of subunit composition across different species.
  • Literature review of identified assembly factors.

Main Results:

  • Plant Complex I is highly conserved, sharing many subunits with mammalian and fungal Complexes I.
  • Plant Complex I possesses additional unique subunits whose functions are not well understood.
  • Only two bona fide assembly factors, GLDH and INDH, have been identified for plant Complex I, contrasting with 14 in humans.

Conclusions:

  • Plant Complex I assembly is a modular and sequential process involving numerous subunits and assembly factors.
  • Further research is needed to elucidate the roles of plant-specific subunits and identify additional assembly factors.
  • Understanding these factors is key to understanding plant energy metabolism and potential therapeutic targets.