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      Supercomplexes in the respiratory chains of yeast and mammalian mitochondria.

      1 ,
      The EMBO journal
      Oxford University Press (OUP)

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          Abstract

          Around 30-40 years after the first isolation of the five complexes of oxidative phosphorylation from mammalian mitochondria, we present data that fundamentally change the paradigm of how the yeast and mammalian system of oxidative phosphorylation is organized. The complexes are not randomly distributed within the inner mitochondrial membrane, but assemble into supramolecular structures. We show that all cytochrome c oxidase (complex IV) of Saccharomyces cerevisiae is bound to cytochrome c reductase (complex III), which exists in three forms: the free dimer, and two supercomplexes comprising an additional one or two complex IV monomers. The distribution between these forms varies with growth conditions. In mammalian mitochondria, almost all complex I is assembled into supercomplexes comprising complexes I and III and up to four copies of complex IV, which guided us to present a model for a network of respiratory chain complexes: a 'respirasome'. A fraction of total bovine ATP synthase (complex V) was isolated in dimeric form, suggesting that a dimeric state is not limited to S.cerevisiae, but also exists in mammalian mitochondria.

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          Author and article information

          Journal
          EMBO J
          The EMBO journal
          Oxford University Press (OUP)
          0261-4189
          0261-4189
          Apr 17 2000
          : 19
          : 8
          Affiliations
          [1 ] Zentrum der Biologischen Chemie, Universitätsklinikum Frankfurt, D-60590 Frankfurt, Germany. schaegger@zbc.klinik-uni-frankfurt.de
          Article
          10.1093/emboj/19.8.1777
          302020
          10775262
          142c6f15-205e-4e40-8824-3f5f5659b7fe
          History

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