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Related Experiment Videos

Electron-proton interactions in terminal oxidases

M Karpefors1, P Adelroth, A Aagaard

  • 1Department of Biochemistry and Biophysics, Göteborg University, Sweden.

Biochimica Et Biophysica Acta
|August 7, 1998
PubMed
Summary

Cytochrome c oxidase uses specific pathways for proton transfer, with the D-pathway crucial for both substrate and pumped protons during oxygen reduction, revising previous understanding.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Bioenergetics

Background:

  • Cytochrome c oxidase acts as a membrane-bound proton pump, coupling electron and proton currents.
  • Understanding the structure-function relationship necessitates investigating individual electron and proton transfer reactions.
  • Proton transfer gating is essential for the coupling mechanism in these enzymes.

Purpose of the Study:

  • To investigate the roles of the K-pathway and D-pathway in proton transfer during cytochrome c oxidase function.
  • To elucidate the mechanism of proton uptake and release coupled to redox reactions.
  • To re-evaluate the function of the D-pathway in proton pumping.

Main Methods:

  • Site-directed mutagenesis to alter specific amino acid residues.

Related Experiment Videos

  • Spectroscopic techniques to monitor reaction kinetics and proton transfer.
  • Analysis of proton uptake and release dynamics at ms and µs timescales.

    • Main Results:

    • Proton uptake/release at heme a3 occurs via the K-pathway on a ms timescale.
    • During O2 reaction, both substrate and pumped protons utilize the D-pathway in a biphasic manner (100 µs and 1 ms).
    • A proton-collecting antenna of carboxylate and histidine residues facilitates rapid proton uptake to the enzyme surface.

    Conclusions:

    • The D-pathway's role extends beyond pumped protons to include substrate proton uptake.
    • Proton transfer pathways are finely tuned for efficient enzyme turnover.
    • Structural features, including histidine networks and electrostatic potentials, support the observed proton transfer dynamics.