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Related Experiment Videos

Multiple conformations of physiological membrane-bound cytochrome c

J D Cortese1, A L Voglino, C R Hackenbrock

  • 1Department of Cell Biology and Anatomy and Laboratories for Cell Biology, The School of Medicine, University of North Carolina, Chapel Hill, North Carolina 27599-7090, USA.

Biochemistry
|June 13, 1998
PubMed
Summary

Cytochrome c (cyt c) binding to mitochondrial membranes changes its structure and electron transport (ET) activity. This study reveals dynamic conformational changes and rapid exchange between soluble and membrane-bound cyt c forms.

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Area of Science:

  • Biochemistry
  • Mitochondrial Biology
  • Protein Conformation

Background:

  • Cytochrome c (cyt c) is crucial for mitochondrial electron transport (ET).
  • A fraction of cyt c remains membrane-bound at physiological ionic strength, with reduced ET activity.
  • Understanding cyt c's membrane interactions is key to mitochondrial function.

Purpose of the Study:

  • To investigate the in vitro formation and properties of membrane-bound cyt c (MB-cyt c).
  • To characterize the conformational changes and ET activity of MB-cyt c under varying ionic conditions.
  • To elucidate the dynamic exchange between soluble and membrane-bound cyt c conformations.

Main Methods:

  • In vitro binding of cyt c to membranes (large and small unilamellar vesicles).

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  • Measurement of electron transport (ET) activity.
  • Circular dichroism spectroscopy to analyze protein secondary structure.
  • Ionic strength and temperature-dependent binding studies.

    • Main Results:

    • Low ionic strength promotes a membrane-bound cyt c (MBL-cyt c) conformation with high ET activity, similar to soluble cyt c.
    • MB-cyt c exhibits decreased alpha-helical content and increased beta-sheet structure.
    • MB-cyt c converts to a more active form on the membrane and releases at physiological ionic strength.
    • Binding and release are dynamic processes influenced by temperature.

    Conclusions:

    • Cyt c exists in soluble and membrane-bound conformations with similar ET activity.
    • These conformations likely undergo rapid interconversion in mitochondria.
    • Soluble proteins can transiently bind to biomembranes, influencing their function.