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Molecular Organization and the Fluid Nature of the Mitochondrial Energy Transducing Membrane

  • Charles R. Hackenbrock
Part of the Nobel Foundation Symposia book series (NOFS, volume 34)

Abstract

The inner or energy transducing membrane of the mitochondrion is the site of various metabolic activities, including the sequential transfer of electrons along a chain of respiratory proteins and the coupling of the free energy derived from such transfer to the phosphorylation of ADP. Electron transfer between the heme protein components of the membrane is rapid and can be expected to require protein-protein interactions equal to the half times of their oxidations, for example, as rapid as 2 msec in the case of the oxidation of cytochrome c by cytochrome c oxidase (Chance et al., 1967). Interactions between other redox components in the membrane, however, may be somewhat slower as indicated by delays in the transfer of reducing equivalents, as for example between the b cytochromes and cytochrome c l and between the flavoproteins and b cytochromes. Of interest in this regard are the reported delays in the rate and half time of ATP synthesis coupled to the rapid half time oxidation of cytochrome c oxidase (Lemasters and Hackenbrock, 1975; Thayer and Hinkle, 1975). Irrespective of such delays, the sequential and rapid events inherent in electron transfer and energy transduction generally tend to support the inference that the proteins in the energy transducing membrane of the mitochondrion are stabilized in a continuous, rigid protein-protein lattice (Fleisher et al., 1967; Sjöstrand and Barajas, 1970; Capaldi and Green, 1972). In classical agreement, the specific proteins of the respiratory chain have been assumed to be ordered with a recurring lateral intermolecular spacing throughout the plane of the membrane (Klingenberg, 1968; Lehninger, 1970). Further, these notions are supported by the fact that the energy transducing membrane is endowed with an unusually high protein content (75%) compared to various other membranes of eukaryote cells.

Keywords

Fracture Face Integral Protein Intramembrane Particle Lipid Phase Transition Cell BioI 
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

© Plenum Press, New York 1977

Authors and Affiliations

  • Charles R. Hackenbrock
    • 1
  1. 1.University of Texas Health Science CenterSouthwestern Medical SchoolDallasUSA

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