Structure of a mitochondrial supercomplex formed by respiratory-chain complexes I and III

被引:249
作者
Dudkina, NV
Eubel, H
Keegstra, W
Boekema, EJ
Braun, HP
机构
[1] Univ Groningen, Groningen Biomol Sci & Biotechnol Inst, Dept Biophys Chem, NL-9747 AG Groningen, Netherlands
[2] Leibniz Univ Hannover, Abt Angew Genet, D-30419 Hannover, Germany
关键词
Arabidopsis; oxidative phosphorylation; respiratory protein complexes; single-particle analysis; plant mitochondria;
D O I
10.1073/pnas.0408870102
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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 F1F0-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+III2 supercomplex.
引用
收藏
页码:3225 / 3229
页数:5
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