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Muhammad A Hagras1

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The succinate-ubiquinone oxidoreductase (SQR) complex acts as an interferometer, using a water channel to enhance electron tunneling for energy production. Changes in mitochondrial volume alter SQR function, impacting cellular respiration and volume regulation.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Bioenergetics

Background:

  • The succinate-ubiquinone oxidoreductase (SQR) complex is crucial for cellular energy production, linking the tricarboxylic acid cycle and electron transport chain.
  • Dysfunction of the SQR complex is implicated in metabolic disorders and diseases like cancer.

Purpose of the Study:

  • To investigate the electron tunneling (ET) pathways within the SQR complex.
  • To explore the role of a newly discovered water channel in SQR function and its response to mitochondrial volume changes.

Main Methods:

  • Calculated ET pathways using the broken-symmetry semi-empirical ZINDO method.
  • Performed molecular dynamics (MD) simulations of the membrane-embedded SQR complex under varying volume conditions (MD_A for regular, MD_B for extended).

Main Results:

  • Identified a water channel between the Fe3S4 and heme b redox centers.
  • Under regular volume (MD_A), ET occurs via two pathways (iron-sulfur cluster chain and heme b), creating an interferometer effect that enhances forward ET.
  • Under extended volume (MD_B), the water channel alters redox center spacing, reducing the SQR equilibrium constant and potentially reversing its function.

Conclusions:

  • The SQR complex functions as an internal interferometer, optimizing electron transfer for succinate oxidation.
  • The water channel plays a key role in sensing mitochondrial volume, regulating SQR activity and potentially restoring mitochondrial function and volume.
  • These findings offer insights into metabolic regulation and potential therapeutic targets for related diseases.