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The ribbon structure of the mitochondrial inner membrane

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Abstract

Electron microscopic evidence is presented for the extensive association of protein subunits into ribbons within the mitochondrial inner membrane. The mitochondrial cristae can be rearranged to a narrow tubular form which exhibits ribbon structure and is fully functional; the morphology of particles derived from submitochondrial electron transport particles by treatment with lysolecithin suggests that the backbone of the ribbon is provided by the cytochrome-free tripartite unit (headpiece, stalk, basepiece) in linear repeat. These results are inconsistent with any single model of the inner membrane previously proposed, but are best understood in terms of a model which combines the concept of an ordered protein continuum with the concept of a fluid lipid bilayer. Further, it is concluded that the “headpiece out” morphology of the tripartite unit represents a viable conformation of the endergonic transducing unit.

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Authors and Affiliations

  1. Institute for Enzyme Research, University of Wisconsin, 53706, Madison, Wisconsin

    Robert A. Haworth, Hirochika Komai & David E. Green

  2. Department of Microbiology, College of Biological Science, University of Guelph, Guelph, Ontario, Canada

    William J. Vail

Authors
  1. Robert A. Haworth
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  2. Hirochika Komai
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  3. David E. Green
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  4. William J. Vail
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Haworth, R.A., Komai, H., Green, D.E. et al. The ribbon structure of the mitochondrial inner membrane. J Bioenerg Biomembr 9, 151–170 (1977). https://doi.org/10.1007/BF00743278

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  • DOI: https://doi.org/10.1007/BF00743278

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