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Cytochrome c binds to lipid domains in arrays of mitochondrial outer membrane channels

Biophysical Journal
|February 1, 1987
PubMed

Insights

Cytochrome c binds to lipid regions of fungal mitochondrial outer membranes, not protein channels. This binding may influence how mitochondria take up apocytochrome c.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Structural Biology

Background:

  • Mitochondrial outer membranes contain protein channels crucial for transport.
  • Cytochrome c is a key protein involved in mitochondrial function and apoptosis.
  • The interaction of cytochrome c with the mitochondrial outer membrane is not fully understood.

Purpose of the Study:

  • To investigate the binding sites of cytochrome c on fungal mitochondrial outer-membrane channels.
  • To determine if cytochrome c interacts with protein or lipid components of the outer membrane.

Main Methods:

  • Computer-averaged electron microscopy was used to analyze negatively stained crystalline arrays.
  • Crystalline arrays of mitochondrial outer-membrane channels were examined with and without cytochrome c (apo- and holo- forms).
  • Stain distribution was analyzed to infer binding interactions.

Main Results:

  • Neither apo- nor holo-cytochrome c significantly altered stain distribution in the protein regions of the channel arrays.
  • Both forms of cytochrome c caused significant stain exclusion from the lipid domains of the arrays.
  • This suggests that cytochrome c binds to the lipid regions of the mitochondrial outer membrane.

Conclusions:

  • Cytochrome c binds to lipid domains on the fungal mitochondrial outer membrane.
  • This binding occurs independently of the protein channel structures.
  • The interaction with exposed phospholipids may play a role in the uptake of apocytochrome c by mitochondria.

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