Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 419-424 |
| Seitenumfang | 6 |
| Fachzeitschrift | Journal of Bioenergetics and Biomembranes |
| Jahrgang | 40 |
| Ausgabenummer | 5 |
| Publikationsstatus | Veröffentlicht - 7 Okt. 2008 |
Abstract
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.
ASJC Scopus Sachgebiete
- Biochemie, Genetik und Molekularbiologie (insg.)
- Physiologie
- Biochemie, Genetik und Molekularbiologie (insg.)
- Zellbiologie
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in: Journal of Bioenergetics and Biomembranes, Jahrgang 40, Nr. 5, 07.10.2008, S. 419-424.
Publikation: Beitrag in Fachzeitschrift › Übersichtsarbeit › Forschung › Peer-Review
}
TY - JOUR
T1 - The higher level of organization of the oxidative phosphorylation system
T2 - Mitochondrial supercomplexes
AU - Dudkina, Natalya V.
AU - Sunderhaus, Stephanie
AU - Boekema, Egbert J.
AU - Braun, Hans Peter
N1 - Funding information: We thank Dr. Roman Kou?il for discussion. We also gratefully acknowledge funding by the Netherlands organization of scientific research (NWO) and by the Deutsche Forschungsge-meinschaft (grants Br1829-7/3 and Br1829-8/1).
PY - 2008/10/7
Y1 - 2008/10/7
N2 - 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.
AB - 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.
KW - Electron microscopy
KW - Mitochondria
KW - Oxidative phosphorylation
KW - Respirasome
KW - Supercomplexes
UR - http://www.scopus.com/inward/record.url?scp=57049094966&partnerID=8YFLogxK
U2 - 10.1007/s10863-008-9167-5
DO - 10.1007/s10863-008-9167-5
M3 - Review article
C2 - 18839290
AN - SCOPUS:57049094966
VL - 40
SP - 419
EP - 424
JO - Journal of Bioenergetics and Biomembranes
JF - Journal of Bioenergetics and Biomembranes
SN - 0145-479X
IS - 5
ER -