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Substrate binding affinity changes in mitochondrial energy-linked reactions

Y Hatefi, T Yagi, D C Phelps

    Proceedings of the National Academy of Sciences of the United States of America
    |March 1, 1982
    PubMed
    Summary
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    Membrane energization alters enzyme conformation, increasing substrate affinity and reaction rates in energy-transducing systems. This study investigated how uncouplers and ionophores affect enzyme kinetics in submitochondrial particles.

    Area of Science:

    • Biochemistry
    • Bioenergetics
    • Mitochondrial Function

    Background:

    • Energy-transducing systems in mitochondria involve complex biochemical reactions.
    • Understanding the kinetics of these reactions is crucial for elucidating cellular energy production mechanisms.

    Purpose of the Study:

    • To investigate the impact of uncouplers and ionophores on the kinetics of energy-linked reactions in submitochondrial particles.
    • To determine how membrane energization affects enzyme-substrate interactions and reaction rates.

    Main Methods:

    • Studied apparent Km and Vmax for oxidative phosphorylation, NTP-33Pi exchange, ATP-driven electron transfer, and respiration-driven transhydrogenation.
    • Utilized uncouplers and valinomycin plus nigericin to perturb membrane energization.
    • Analyzed kinetic data by plotting ln (Vmax/Km) against perturbant concentration.

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    Main Results:

    • Partial uncoupling decreased apparent Vmax and increased apparent Km for all studied reactions.
    • A linear decrease in ln (Vmax/Km) was observed with increasing perturbant concentration (decreasing free energy).

    Conclusions:

    • Membrane energization induces conformational changes in enzymes, enhancing enzyme-substrate affinity.
    • These conformational changes facilitate reaction rates in energy-transducing systems.
    • Findings provide insights into the mechanism of action of mitochondrial energy transduction.