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Related Experiment Videos

Crystallization of cytochrome bc1 complex.

T Ozawa, M Tanaka, Y Shimomura

    Proceedings of the National Academy of Sciences of the United States of America
    |February 1, 1983
    PubMed
    Summary

    Beef heart Complex III was purified and crystallized, revealing nine polypeptide subunits and a hexagonal crystal structure. Bound cardiolipin plays a role in the structural integrity of this crucial mitochondrial respiratory complex.

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    Area of Science:

    • Biochemistry
    • Mitochondrial respiration
    • Protein purification

    Background:

    • Complex III (cytochrome bc1 particle) is essential for cellular respiration.
    • Understanding its structure is key to understanding energy production.

    Purpose of the Study:

    • To purify and crystallize Complex III from beef heart mitochondria.
    • To characterize the subunit composition and structural properties of the purified complex.

    Main Methods:

    • Purification using hydrophobic interaction and affinity chromatography.
    • NaDodSO4 gel electrophoresis for subunit analysis.
    • Crystallization via slow detergent removal.
    • Electron microscopy and diffraction for structural determination.

    Main Results:

    • A purified Complex III sample retained 7 mol cardiolipin per mol cytochrome c1.
    • Nine polypeptide subunits were identified.
    • The complex has an estimated molecular weight of ~225,000.
    • Hexagonal crystals with specific unit cell dimensions were obtained.

    Conclusions:

    • Complex III can be purified and crystallized, enabling structural studies.
    • Bound cardiolipin is likely important for the structural integrity of Complex III.
    • The determined crystal structure provides a basis for further functional and structural investigations.

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