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Biophysical Journal 51: 221-226 (1987)
© 1987 the Biophysical Society

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

C A Mannella, A J Ribeiro and J Frank

ABSTRACT

Computer-averaged electron microscopic images of negatively stained crystalline arrays of fungal mitochondrial outer-membrane channels in the presence and absence of cytochrome c were compared. Neither the apo- nor the holo- forms of cytochrome c significantly changed the stain distribution in the protein regions of the channel arrays. However, both forms of cytochrome c caused significant stain exclusion from the lipid domains in the arrays, suggesting binding of the polypeptides at these loci. The implications of binding of apocytochrome c to clusters of exposed phospholipids on the mitochondrial outer membrane are discussed with respect to the mechanism of uptake of this polypeptide by mitochondria.




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S. Stanley, J. A. Dias, D. D'Arcangelis, and C. A. Mannella
Peptide-specific Antibodies as Probes of the Topography of the Voltage-gated Channel in the Mitochondrial Outer Membrane of Neurospora crassa
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Copyright © 1987 by the Biophysical Society.