In:
Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 102, No. 9 ( 2005-03), p. 3225-3229
Abstract:
Mitochondria are central to the efficient provision of energy for eukaryotic cells. The oxidative-phosphorylation system of mitochondria consists of a series of five major membrane complexes: NADH–ubiquinone oxidoreductase (commonly known as complex I), succinate–ubiquinone oxidoreductase (complex II), ubiquinol–cytochrome c oxidoreductase (cytochrome bc 1 complex or complex III), cytochrome c –O 2 oxidoreductase (complex IV), and F 1 F 0 –ATP synthase (complex V). Several lines of evidence have recently suggested that complexes I and III–V might interact to form supercomplexes. However, because of their fragility, the structures of these supercomplexes are still unknown. A stable supercomplex consisting of complex I and dimeric complex III was purified from plant mitochondria. Structural characterization by single-particle EM indicates a specific type of interaction between monomeric complex I and dimeric complex III in a 1:1 ratio. We present a model for how complexes I and III are spatially organized within the I+III 2 supercomplex.
Type of Medium:
Online Resource
ISSN:
0027-8424
,
1091-6490
DOI:
10.1073/pnas.0408870102
Language:
English
Publisher:
Proceedings of the National Academy of Sciences
Publication Date:
2005
detail.hit.zdb_id:
209104-5
detail.hit.zdb_id:
1461794-8
SSG:
11
SSG:
12
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