Details
| Original language | English |
|---|---|
| Pages (from-to) | 232-240 |
| Number of pages | 9 |
| Journal | Trends in plant science |
| Volume | 11 |
| Issue number | 5 |
| Publication status | Published - 17 Apr 2006 |
Abstract
The intricate, heavily folded inner membrane of mitochondria houses the respiratory chain complexes. These complexes, together with the ATP synthase complex, are responsible for energy production, which is stored as ATP. The structure of the individual membrane-bound protein components has been well characterized. In particular, the use of Blue-native polyacrylamide gel electrophoresis has been instrumental in recent years in providing evidence that these components are organized into supercomplexes. Single particle electron microscopy studies have enabled a structural characterization of some of the mitochondrial supercomplexes. This has provided the opportunity to define a functional role for these supercomplexes for the first time, in particular for the dimeric ATP synthase complex, which appears to be responsible for the folding of the inner mitochondrial membrane.
ASJC Scopus subject areas
- Agricultural and Biological Sciences(all)
- Plant Science
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In: Trends in plant science, Vol. 11, No. 5, 17.04.2006, p. 232-240.
Research output: Contribution to journal › Review article › Research › peer review
}
TY - JOUR
T1 - Respiratory chain supercomplexes in the plant mitochondrial membrane
AU - Dudkina, Natalya V.
AU - Heinemeyer, Jesco
AU - Sunderhaus, Stephanie
AU - Boekema, Egbert J.
AU - Braun, Hans Peter
N1 - Funding information: This work was supported by the Deutsche Forschungsgemeinschaft and the Dutch science foundation NWO-CW.
PY - 2006/4/17
Y1 - 2006/4/17
N2 - The intricate, heavily folded inner membrane of mitochondria houses the respiratory chain complexes. These complexes, together with the ATP synthase complex, are responsible for energy production, which is stored as ATP. The structure of the individual membrane-bound protein components has been well characterized. In particular, the use of Blue-native polyacrylamide gel electrophoresis has been instrumental in recent years in providing evidence that these components are organized into supercomplexes. Single particle electron microscopy studies have enabled a structural characterization of some of the mitochondrial supercomplexes. This has provided the opportunity to define a functional role for these supercomplexes for the first time, in particular for the dimeric ATP synthase complex, which appears to be responsible for the folding of the inner mitochondrial membrane.
AB - The intricate, heavily folded inner membrane of mitochondria houses the respiratory chain complexes. These complexes, together with the ATP synthase complex, are responsible for energy production, which is stored as ATP. The structure of the individual membrane-bound protein components has been well characterized. In particular, the use of Blue-native polyacrylamide gel electrophoresis has been instrumental in recent years in providing evidence that these components are organized into supercomplexes. Single particle electron microscopy studies have enabled a structural characterization of some of the mitochondrial supercomplexes. This has provided the opportunity to define a functional role for these supercomplexes for the first time, in particular for the dimeric ATP synthase complex, which appears to be responsible for the folding of the inner mitochondrial membrane.
UR - http://www.scopus.com/inward/record.url?scp=33646377888&partnerID=8YFLogxK
U2 - 10.1016/j.tplants.2006.03.007
DO - 10.1016/j.tplants.2006.03.007
M3 - Review article
C2 - 16616870
AN - SCOPUS:33646377888
VL - 11
SP - 232
EP - 240
JO - Trends in plant science
JF - Trends in plant science
SN - 1360-1385
IS - 5
ER -