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Related Experiment Videos

Modulation of proton pumping efficiency in bacterial ATP synthases.

Paola Turina1, Alberto Rebecchi, Manuela D'Alessandro

  • 1Department of Biology, Laboratory of Biochemistry and Biophysics, University of Bologna, Via Irnerio 42, 40126 Bologna, Italy.

Biochimica Et Biophysica Acta
|June 13, 2006
PubMed
Summary

ADP and phosphate regulate ATP synthase function in bacteria. Depletion of these molecules leads to inefficient proton pumping, suggesting a switch between tightly and loosely coupled states.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Bioenergetics

Background:

  • ATP synthase facilitates proton transport across membranes coupled to ATP hydrolysis.
  • The regulation of ATP synthase efficiency by substrate availability is crucial for cellular energy production.

Purpose of the Study:

  • To investigate the role of ADP and phosphate concentrations in regulating the coupling efficiency of ATP synthase in Rhodobacter caspulatus and Escherichia coli.
  • To determine the apparent dissociation constants (Kd) for ADP and phosphate binding to ATP synthase.

Main Methods:

  • Utilized ATP regenerating systems to deplete ADP and measured transmembrane pH differences (DeltapH).
  • Assessed proton uptake and ATP hydrolysis rates under varying ADP and phosphate concentrations.
  • Calculated clamped ADP concentrations and estimated Kd values.

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Main Results:

  • ADP depletion significantly reduced steady-state DeltapH in Rhodobacter caspulatus, with an estimated Kd of ~0.5 microM for ADP.
  • Proton uptake was dependent on phosphate concentration (Kd ~70 microM) in Rhodobacter caspulatus.
  • In Escherichia coli, Pi inhibited hydrolysis, an effect suppressed by ADP depletion; both ADP and Pi showed mutual dependence.
  • Proton pumping was less sensitive to ADP and Pi than hydrolysis, showing stimulation at intermediate concentrations.

Conclusions:

  • ADP and phosphate act as crucial ligands that induce a functional state of ATP synthase for tightly coupled proton pumping.
  • Depletion of ADP or phosphate favors an inefficient (slipping) functional state of ATP synthase.
  • These functional state switches are likely mediated by structural changes in the epsilon-subunit of ATP synthase.