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Ionic strength effects on cytochrome aa3 kinetics.

J Wilms, E C Veerman, B W König

    Biochimica Et Biophysica Acta
    |March 12, 1981
    PubMed
    Summary
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    Optimal ionic strength balances cytochrome c-aa3 affinity and complex formation for steady-state activity. Polylysine and cytochrome c may stimulate release from the complex, indicating negative cooperativity.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Enzyme Kinetics

    Background:

    • Cytochrome c oxidase (cytochrome aa3) is crucial for cellular respiration.
    • Understanding its interaction with cytochrome c is key to elucidating electron transfer mechanisms.

    Purpose of the Study:

    • To investigate the role of ionic strength on cytochrome c-cytochrome aa3 complex activity.
    • To characterize the binding kinetics and cooperativity between cytochrome c and cytochrome aa3.

    Main Methods:

    • Pre-steady-state kinetic measurements to determine reaction rates.
    • Analysis of enzyme-inhibitor interactions to infer binding affinities.
    • Ionic strength dependence studies.

    Main Results:

    Related Experiment Videos

    • An optimal ionic strength exists for cytochrome aa3 activity, influenced by competing affinity and complex formation effects.
    • At low ionic strength, electron transfer occurs via unbound cytochrome c, with charged interactions facilitating transfer between cytochromes c1 and aa3.
    • Polylysine and potentially cytochrome c stimulate the release of bound cytochrome c, suggesting negative cooperativity between binding sites.
    • Dissociation constants for high (0.6 nM) and low (20 microM) affinity sites on cytochrome aa3 were estimated at 8.8 mM ionic strength.

    Conclusions:

    • Ionic strength critically modulates cytochrome c-cytochrome aa3 interactions and overall enzyme activity.
    • The findings reveal complex binding dynamics and electron transfer pathways involving cytochrome c.
    • Evidence for negative cooperativity in cytochrome c binding to cytochrome aa3 was observed.