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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...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Springer US
2008
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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. |
format | Text |
id | pubmed-2780661 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | Springer US |
record_format | MEDLINE/PubMed |
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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