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J. Biol. Chem., Vol. 282, Issue 16, 12240-12248, April 20, 2007

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A Structural Model of the Cytochrome c Reductase/Oxidase Supercomplex from Yeast Mitochondria^*

Jesco Heinemeyer, Hans-Peter Braun¹, Egbert J. Boekema², and Roman Kouil³

From the Institute for Plant Genetics, Faculty of Natural Sciences, Universität Hannover, Herrenhäuser Strasse 2, 30419 Hannover, Germany and the Department of Biophysical Chemistry, GBB, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands

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 15Å 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 40Å 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.

Received for publication, November 13, 2006 , and in revised form, January 29, 2007.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Supported by a grant from the Deutsche Forschungsgemeinschaft (Br1829-7/2).

² To whom correspondence may be addressed. Tel.: 31-50-3634225; Fax: 31-50-3634800; E-mail: e.j.boekema{at}rug.nl.

³ Supported by grants from the Dutch Science Foundation Netherlands Organization for Scientific Research, Council for Chemical Sciences (NWO-CW). To whom correspondence may be addressed. Tel.: 31-50-3634225; Fax: 31-50-3634800; E-mail: r.kouril{at}rug.nl.

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