Abstract
A steadily increasing number of physiological, biochemical, and structural studies have provided a growing support to the notion that the respiratory electron transfer chain may contain supra-molecular edifices made of the assembly of some, if not all, of its individual links. This structure, usually referred to as the solid state model—in comparison to the liquid state model in which the electron transfer reactions between the membrane bound enzymes are diffusion controlled—is seen as conferring specific kinetic properties to the chain and thus as being highly relevant from a functional point of view. Although the assumption that structural changes are mirrored by functional adjustment is undoubtedly legitimate, experimental evidences supporting it remain scarce. Here we review a recent methodological development aimed at tackling the functional relevance of the supramolecular organization of the respiratory electron transfer chain in intact cells.
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Acknowledgements
Warm acknowledgements are due to Daniel Béal and Martin Trouillard without whom the photo-activated respiratory electron transfer chain would have remained a project. This work was supported by CNRS, by the ANR (ANR-07-BLAN-0360-01), and by the “Initiative d’Excellence” program from the French State (Grant “DYNAMO”, ANR-11-LABX-0011-01).
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Rappaport, F. (2015). A Method Aimed at Assessing the Functional Consequences of the Supramolecular Organization of the Respiratory Electron Transfer Chain by Time-Resolved Studies. In: Palmeira, C., Rolo, A. (eds) Mitochondrial Regulation. Methods in Molecular Biology, vol 1241. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-1875-1_9
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DOI: https://doi.org/10.1007/978-1-4939-1875-1_9
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