The higher level of organization of the oxidative phosphorylation system: mitochondrial supercomplexes.
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.
Electron microscopy group, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, AG, Groningen, The Netherlands.
Natalya V
NV
Dudkina
Stephanie
S
Sunderhaus
Egbert J
EJ
Boekema
Hans-Peter
HP
Braun
D000818:Animals; D045222:Electron Transport Chain Complex Proteins / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure; D004591:Electrophoresis, Polyacrylamide Gel; D008854:Microscopy, Electron; D008928:Mitochondria / Q000201:enzymology*; D025261:Mitochondrial Proton-Translocating ATPases / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D008954:Models, Biological; D008958:Models, Molecular; D010085:Oxidative Phosphorylation; D020836:Protein Structure, Quaternary
D045222:Electron Transport Chain Complex Proteins; D025261:Mitochondrial Proton-Translocating ATPases