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The higher level of organization of the oxidative phosphorylation system: mitochondrial supercomplexes

Natalya V. DudkinaElectron microscopy group, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, AG, Groningen, The NetherlandsStephanie SunderhausInstitute for Plant Genetics, Faculty of Natural Sciences, Leibniz Universität Hannover, Herrenhäuser Str. 2, 30419, Hannover, GermanyEgbert J. BoekemaElectron microscopy group, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The NetherlandsHans‐Peter BraunInstitute for Plant Genetics, Faculty of Natural Sciences, Leibniz Universität Hannover, Herrenhäuser Str. 2, 30419, Hannover, Germany
2008en
ABI

Аннотация

The organization of the oxidative phosphorylation (OXPHOS) system within the inner mitochondrial membrane appears to be far more complicated than previously thought. In particular, the individual protein complexes of the OXPHOS system (complexes I to V) were found to specifically interact forming defined supramolecular structures. Blue-native polyacrylamide gel electrophoresis and single particle electron microscopy proved to be especially valuable in studying the so-called "respiratory supercomplexes". Based on these procedures, increasing evidence was presented supporting a "solid state" organization of the OXPHOS system. Here, we summarize results on the formation, organisation and function of the various types of mitochondrial OXPHOS supercomplexes.

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