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J. Biol. Chem., Vol. 276, Issue 38, 35231-35234, September 21, 2001
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,
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,

, and
From the Bifurcated electron flow to high potential
"Rieske" iron-sulfur cluster and low potential heme
bL is crucial for respiratory energy
conservation by the cytochrome bc1 complex. The
chemistry of ubiquinol oxidation has to ensure the thermodynamically
unfavorable electron transfer to heme bL. To
resolve a central controversy about the number of ubiquinol molecules
involved in this reaction, we used high resolution magic-angle-spinning
nuclear magnetic resonance experiments to show that two out of three
n-decyl-ubiquinones bind at the ubiquinol oxidation center
of the complex. This substantiates a proposed mechanism in which a
charge transfer between a ubiquinol/ubiquinone pair explains the
bifurcation of electron flow.
Johann Wolfgang Goethe-Universität
Frankfurt, Institut für Organische Chemie, Marie-Curie-Strasse
11, D-60439 Frankfurt am Main, Germany, the Max Planck Institute for
Biophysical Chemistry, Am Fassberg 11, D-37077 Göttingen,
Germany, the § Universitätsklinikum Frankfurt,
Institut für Biochemie I, D-60590 Frankfurt am Main, Germany, the
¶ Max-Planck-Institut für Biophysik, Abteilung für
Molekulare Membranbiologie, Heinrich-Hoffmann-Strasse 7, D-60528
Frankfurt am Main, Germany,
Bruker Analytik GmbH, Silberstreifen
4, D-76287 Rheinstetten, Germany, and the ** Department of Biochemistry
and Molecular Biology, Oklahoma State University,
Stillwater, Oklahoma 74078
The on-line version of this article (http://www.jbc.org)
contains a table.

To whom correspondence may be addressed. Tel.:
49-69/63016926, Fax: 49-69/63016970; E-mail:
brandt@zbc.klinik.uni-frankfurt.de (for U. B.); Tel.:
49-69/79829130, Fax: 49-69/79829128, E-mail: cigr@org.chemie.uni-frankfurt.de (for C. G.); Tel.:
405-744-6612, Fax: 405-744-7799, E-mail: cayuq@okstate.edu (for
C.-A. Y.).
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