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Potentiometric studies on yeast complex III.

A L T'sai, G Palmer

    Biochimica Et Biophysica Acta
    |February 17, 1983
    PubMed
    Summary
    This summary is machine-generated.

    Researchers measured redox potentials in yeast Complex III using potentiometry. They found temperature-dependent shifts in cytochrome b potentials and identified a conformational change in the iron-sulfur center upon reduction.

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    Area of Science:

    • Biochemistry
    • Bioenergetics
    • Enzyme kinetics

    Background:

    • Mitochondrial Complex III (cytochrome bc1 complex) is crucial for cellular respiration.
    • Understanding the redox potentials of its components is key to elucidating electron transfer mechanisms.

    Purpose of the Study:

    • To determine the midpoint redox potentials of cytochromes b and c1, the iron-sulfur center, and ubiquinone in yeast Complex III.
    • To investigate the influence of temperature, pH, and detergents on these potentials.

    Main Methods:

    • Potentiometric titrations using room-temperature MCD and low-temperature EPR spectroscopy.
    • Monitoring semiquinone radical signals for ubiquinone potential determination.

    Main Results:

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  • Cytochrome c1 midpoint potential was 270 mV and pH-independent.
  • Cytochrome b potentials varied with temperature (e.g., 62/-20 mV at room temp vs. 116/-4 mV at 10 K).
  • Iron-sulfur center potential was 286 mV, with a conformational change upon reduction. Ubiquinone potentials also showed temperature dependence.

    • Conclusions:

    • Temperature significantly impacts cytochrome b redox states in yeast Complex III.
    • Detergent choice influences cytochrome b potentials and EPR signals.
    • Antimycin induces a ubiquinone-mediated transition of low-potential to high-potential cytochrome b heme.