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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 de...

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Detalles Bibliográficos
Autores principales: Dudkina, Natalya V., Sunderhaus, Stephanie, Boekema, Egbert J., Braun, Hans-Peter
Formato: Texto
Lenguaje:English
Publicado: Springer US 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2780661/
https://www.ncbi.nlm.nih.gov/pubmed/18839290
http://dx.doi.org/10.1007/s10863-008-9167-5
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author Dudkina, Natalya V.
Sunderhaus, Stephanie
Boekema, Egbert J.
Braun, Hans-Peter
author_facet Dudkina, Natalya V.
Sunderhaus, Stephanie
Boekema, Egbert J.
Braun, Hans-Peter
author_sort Dudkina, Natalya V.
collection PubMed
description 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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spelling pubmed-27806612009-11-23 The higher level of organization of the oxidative phosphorylation system: mitochondrial supercomplexes Dudkina, Natalya V. Sunderhaus, Stephanie Boekema, Egbert J. Braun, Hans-Peter J Bioenerg Biomembr Article 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. Springer US 2008-10-07 2008-10 /pmc/articles/PMC2780661/ /pubmed/18839290 http://dx.doi.org/10.1007/s10863-008-9167-5 Text en © The Author(s) 2008
spellingShingle Article
Dudkina, Natalya V.
Sunderhaus, Stephanie
Boekema, Egbert J.
Braun, Hans-Peter
The higher level of organization of the oxidative phosphorylation system: mitochondrial supercomplexes
title The higher level of organization of the oxidative phosphorylation system: mitochondrial supercomplexes
title_full The higher level of organization of the oxidative phosphorylation system: mitochondrial supercomplexes
title_fullStr The higher level of organization of the oxidative phosphorylation system: mitochondrial supercomplexes
title_full_unstemmed The higher level of organization of the oxidative phosphorylation system: mitochondrial supercomplexes
title_short The higher level of organization of the oxidative phosphorylation system: mitochondrial supercomplexes
title_sort higher level of organization of the oxidative phosphorylation system: mitochondrial supercomplexes
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2780661/
https://www.ncbi.nlm.nih.gov/pubmed/18839290
http://dx.doi.org/10.1007/s10863-008-9167-5
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