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ATP synthesis at physiological nucleotide concentrations.

Axel Meyrat1, Christoph von Ballmoos2

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High ATP concentrations inhibit ATP synthesis by F1F0 ATP synthase, even under strong proton motive force. The ATP/ADP ratio, not ATP hydrolysis, controls this product inhibition in bacteria.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Microbiology

Background:

  • F1F0 ATP synthase synthesizes ATP using proton motive force (pmf) in mitochondria and bacteria.
  • The enzyme can also function as a proton pump driven by ATP hydrolysis when pmf is absent.
  • Understanding ATP synthesis regulation under physiological conditions, like high pmf and ATP levels, is crucial.

Purpose of the Study:

  • To investigate the effect of high ATP concentrations on F1F0 ATP synthase activity under conditions of high pmf.
  • To determine the mechanism by which ATP affects ATP synthesis rate in bacteria.

Main Methods:

  • Development of a modified luminescence-based assay using adenosine 5'-O-(1-thiotriphosphate) (ATPαS) to measure ATP synthesis.
  • Utilized inverted membrane vesicles from E. coli.
  • Tested the effects of varying ATPαS, ADP, and inorganic phosphate (Pi) concentrations under saturating pmf.

Main Results:

  • High concentrations of ATPαS (5 mM) reduced ATP synthesis to approximately 10% of the maximal rate under saturating pmf.
  • This inhibition was reversed by adding ADP, but not Pi, indicating the ATP/ADP ratio's role.
  • The ATP/ADP ratio in growing E. coli (~30) was found to limit ATP synthesis to about 20% of the maximum possible rate.

Conclusions:

  • The ATP/ADP ratio acts as a key regulator of F1F0 ATP synthase activity under high pmf conditions.
  • Product inhibition by ATP, influenced by the ATP/ADP ratio, limits the rate of ATP synthesis.
  • This regulation occurs via product inhibition, not an increased rate of ATP hydrolysis.