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Relationships Between Bilayer Lipid, Motional Freedom of Oxidoreductase Components, and Electron Transfer in the Mitochondrial Inner Membrane

  • Charles R. Hackenbrock
  • Heinz Schneider
  • John J. Lemasters
  • Matthias Höchli

Abstract

The relationships between bilayer lipid, diffusional and conformational activities of oxidoreduction components, and electron transfer activity in the mitochondrial inner membrane are considered. Using a new, low pH method to fuse liposome phospholipid (asolectin) with the isolated mitochondrial inner membrane, the membrane bilayer is enriched up to 700% with exogenous phospholipid. During such enrichment, ultrastructural analysis reveals that integral proteins diffuse freely and randomly into the expanding bilayer. Kinetic analysis reveals that a diffusion limited step occurs between succinate- and NADH dehydrogenase and cytochromes bc l, and that the dehydrogenases, ubiquinone, and cytochromes bc l are free to diffuse independently of one another in the membrane plane. Whether cytochromes bc l and cytochrome c oxidase codiffuse in the membrane plane, or diffuse independently of one another remains unclear. The specific activities of succinate- and NADH-dehydrogenase as well as cytochrome c oxidase are affected by bilayer enrichment. This most likely occurs through the direct modulation by the newly incorporated phospholipid on conformational activity required in the oxidoreductases for electron transfer.

Keywords

Lateral Diffusion NADH Dehydrogenase Membrane Bilayer Integral Protein Membrane Plane 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1980

Authors and Affiliations

  • Charles R. Hackenbrock
    • 1
  • Heinz Schneider
    • 1
  • John J. Lemasters
    • 1
  • Matthias Höchli
    • 1
  1. 1.Laboratories for Cell Biology, Department of Anatomy, School of MedicineUniversity of North CarolinaChapel HillUSA

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