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Related Experiment Videos

Electrogenic transport by the Enterococcus hirae ATPase.

H J Apell1, M Solioz

  • 1Department of Biology, University of Konstanz, F.R.G.

Biochimica Et Biophysica Acta
|June 26, 1990
PubMed
Summary
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Researchers studied a transport ATPase from Enterococcus hirae, finding it acts as a proton pump. This proton ATPase translocates protons, influenced by pH, suggesting cytoplasmic proton concentration regulation.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Membrane Transport

Background:

  • Enterococcus hirae possesses a transport ATPase involved in cellular processes.
  • Understanding the mechanism of this ATPase is crucial for elucidating bacterial energy transduction.

Purpose of the Study:

  • To investigate the electrogenic action of the Enterococcus hirae transport ATPase.
  • To determine the role of pH and ionic composition on ATPase activity.

Main Methods:

  • Reconstitution of the transport ATPase into lipid vesicles.
  • Utilizing the fluorescent dye oxonol VI to probe membrane potential.
  • Varying extravesicular pH and ionic composition to assess ATPase function.

Main Results:

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  • The reconstituted ATPase generated an intravesicularly positive potential, indicating electrogenic transport.
  • Extravesicular pH significantly affected pumping rate and duration; neutral pH resulted in transient activity, while pH 5.6 showed continuous pumping.
  • Transport activity was independent of buffer ionic composition.

Conclusions:

  • The findings support the interpretation of the enzyme as a proton ATPase.
  • The enzyme's activity appears regulated by cytoplasmic proton concentration.
  • Protons are electrogenically translocated from the cytoplasm to the extracellular space.