A structural model of the cytochrome c reductase/oxidase supercomplex from yeast mitochondria

被引:127
作者
Heinemeyer, Jesco
Braun, Hans-Peter
Boekema, Egbert J.
Kouril, Roman
机构
[1] Univ Groningen, GBB, Dept Biophys Chem, NL-9747 AG Groningen, Netherlands
[2] Leibniz Univ Hannover, Fac Nat Sci, Inst Plant Genet, D-30419 Hannover, Germany
关键词
D O I
10.1074/jbc.M610545200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Mitochondrial respiratory chain complexes are arranged in supercomplexes within the inner membrane. Interaction of cytochrome c reductase ( complex III) and cytochrome c oxidase ( complex IV) was investigated in Saccharomyces cerevisiae. Projection maps at 15 angstrom resolution of supercomplexes III2 + IV1 and III2 + IV2 were obtained by electron microscopy. Based on a comparison of our maps with atomic x-ray structures for complexes III and IV we present a pseudo-atomic model of their precise interaction. Two complex IV monomers are specifically attached to dimeric complex III with their convex sides. The opposite sides, which represent the complex IV dimer interface in the x-ray structure, are open for complex IV-complex IV interactions. This could lead to oligomerization of III2 + IV2 supercomplexes, but this was not detected. Instead, binding of cytochrome c to the supercomplexes was revealed. It was calculated that cytochrome c has to move less than 40 angstrom at the surface of the supercomplex for electron transport between complex III2 and complex IV. Hence, the prime function of the supercomplex III2 + IV2 is proposed to be a scaffold for effective electron transport between complexes III and IV.
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收藏
页码:12240 / 12248
页数:9
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