Structure of a mitochondrial supercomplex formed by respiratory-chain complexes I and III
- authored by
- Natalia V. Dudkina, Holger Eubel, Wilko Keegstra, Egbert J. Boekema, Hans Peter Braun
- 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 bc1 complex or complex III), cytochrome c-O2 oxidoreductase (complex IV), and F 1F0-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.
- Organisation(s)
-
Institute of Plant Genetics
- External Organisation(s)
-
University of Groningen
- Type
- Article
- Journal
- Proceedings of the National Academy of Sciences of the United States of America
- Volume
- 102
- Pages
- 3225-3229
- No. of pages
- 5
- ISSN
- 0027-8424
- Publication date
- 03.2005
- Publication status
- Published
- Peer reviewed
- Yes
- ASJC Scopus subject areas
- General
- Electronic version(s)
-
https://doi.org/10.1073/pnas.0408870102 (Access:
Open)
