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Updated: Oct 23, 2025

High-Resolution Respirometry to Assess Bioenergetics in Cells and Tissues Using Chamber- and Plate-Based Respirometers
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Electron Transfer Coupled to Conformational Dynamics in Cell Respiration.

Marco Reidelbach1, Christoph Zimmer2, Brigitte Meunier3

  • 1Department of Physics, University of Helsinki, Helsinki, Finland.

Frontiers in Molecular Biosciences
|August 23, 2021
PubMed
Summary

Cytochrome c oxidase (CcO) couples electron transfer to proton pumping for ATP synthesis. This study reveals a dynamic region in helix X is crucial for optimizing electron transfer in CcO.

Keywords:
density functional theorymitochondrial respirationmolecular dynamics simulationsproton pumpingyeast bioenergetics

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Bioenergetics

Background:

  • Cellular respiration generates energy via electron transport chains.
  • Cytochrome c oxidase (CcO) is the terminal enzyme, coupling redox reactions to proton pumping for ATP synthesis.
  • The precise mechanism linking electron transfer to proton pumping in mammalian CcO remains incompletely understood.

Purpose of the Study:

  • To investigate the role of a conserved dynamic region in transmembrane helix X of CcO subunit I.
  • To determine if this region couples electron transfer to proton translocation in mammalian CcO.
  • To compare the function of this region in yeast and bovine CcO.

Main Methods:

  • Generation of yeast CcO mutants (V380M and G384D) in helix X.
  • Assessment of respiratory deficiency and CcO turnover in mutant strains.
  • Long-timescale atomistic molecular dynamics simulations of wild-type and mutant bovine and yeast CcOs.

Main Results:

  • Yeast CcO mutants exhibited respiratory deficiency due to inhibited intra-protein electron transfer and CcO turnover.
  • Molecular dynamics simulations revealed redox- and mutation-dependent conformational changes in the TMH X span.
  • These dynamic changes in helix X were observed in both bovine and yeast CcO.

Conclusions:

  • The dynamic module within TMH X plays a critical role in optimizing intra-protein electron transfer in CcO.
  • Conformational flexibility in this region is essential for efficient CcO function.
  • This finding provides insights into the mechanistic differences between mammalian and bacterial CcO.