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PH-jump-induced ADP phosphorylation in mitochondria

I V Malenkova, S P Kuprin, R M Davydov

    Biochimica Et Biophysica Acta
    |October 18, 1982
    PubMed
    Summary

    Mitochondria can generate ATP after a rapid external pH increase, but not decrease. Optimal ATP synthesis occurs when pH jumps over 0.7 units, crossing 8.1-8.3, and is blocked by oligomycin.

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    Biochemistry·1997

    Area of Science:

    • Mitochondrial biology
    • Bioenergetics
    • Cellular respiration

    Background:

    • Mitochondria are crucial for cellular energy production through oxidative phosphorylation.
    • Mitochondrial function can be impaired by factors such as aging and physical stress like freeze-thaw cycles.
    • Uncoupling of oxidative phosphorylation disrupts the normal ATP synthesis pathway.

    Purpose of the Study:

    • To investigate the conditions under which uncoupled mitochondria can synthesize ATP.
    • To determine the parameters of external pH changes that induce ATP synthesis.
    • To characterize the mechanism of pH-jump-induced ATP synthesis.

    Main Methods:

    • Utilized isolated mitochondria subjected to aging or freeze-thaw treatments.
    • Applied rapid changes in external pH (pH jumps) to mitochondrial suspensions.
    • Measured ATP synthesis in response to pH gradients.
    • Assessed the effect of oligomycin on pH-jump-induced ATP synthesis.

    Main Results:

    • Uncoupled mitochondria synthesized ATP following a rapid increase, but not a decrease, in external pH.
    • Maximal ATP yield (approx. 2.5 ATP/electron-transport chain) was achieved when the pH jump exceeded 0.7 units and crossed the 8.1-8.3 range.
    • Oligomycin completely inhibited this pH-jump-induced ATP synthesis, indicating reliance on ATP synthase.

    Conclusions:

    • Mitochondrial ATP synthesis can be driven by artificial proton gradients generated by rapid external pH increases.
    • The efficiency of this process is dependent on the magnitude and trajectory of the pH change.
    • The involvement of the F1F0-ATP synthase complex is confirmed by oligomycin inhibition.

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