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Related Experiment Videos

Redox-driven proton pumping by heme-copper oxidases.

Peter Brzezinski1, Gisela Larsson

  • 1Department of Biochemistry and Biophysics, The Arrhenius Laboratories for Natural Sciences, Stockholm University, Svante Arrhenius vag 12, SE-106 91, Stockholm, Sweden. peterb@dbb.su.se

Biochimica Et Biophysica Acta
|August 9, 2003
PubMed
Summary

Heme-copper oxidases pump protons using electron transfer to reduce oxygen. A proposed model explains how energy from this process drives proton translocation across membranes via structural changes.

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Area of Science:

  • Molecular bioenergetics
  • Enzymology
  • Membrane protein function

Background:

  • Heme-copper oxidases are integral membrane proteins crucial for cellular respiration.
  • Proton translocation is coupled to electron transfer from donors like cytochrome c to oxygen.
  • Understanding the molecular mechanisms of these redox-driven proton pumps is a key challenge.

Purpose of the Study:

  • To elucidate the molecular mechanism of proton pumping in heme-copper oxidases.
  • To present a novel model for energy conservation during oxygen reduction and proton transfer.
  • To investigate the role of specific residues and structural changes in proton translocation.

Main Methods:

  • Analysis of enzyme structure and function.
  • Biochemical assays to study electron transfer and proton pumping.

Related Experiment Videos

  • Computational modeling to understand energy transduction.
  • Main Results:

    • Proton pumping is linked to exergonic steps in oxygen reduction to water.
    • High pKa proton acceptors are generated at the catalytic site during oxygen reduction.
    • Deprotonation of specific residues, like glutamate E(I-286) in Rhodobacter sphaeroides cytochrome c oxidase, induces structural changes.
    • These structural changes propagate to the proton output side, facilitating proton transfer.

    Conclusions:

    • A novel proton-pumping model is proposed, conserving free energy from oxygen reduction.
    • Structural changes initiated by residue deprotonation are key to coupling electron transfer with proton translocation.
    • The model explains how protons are accepted from the input side and released to the output side of the membrane.