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J. Biol. Chem., Vol. 277, Issue 7, 4605-4608, February 15, 2002
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From the The bifurcated reaction at the
Qo-site of the bc1 complex
provides the mechanistic basis of the proton pumping activity through which the complex conserves redox energy in the proton gradient. Structural information about the binding of quinone at the site is
lacking, because the site is vacant in crystals of the native complexes. We now report the first structural characterization of the
interaction of the native quinone occupant with the Rieske iron-sulfur
protein in the bc1 complex of Rhodobacter
sphaeroides, using high resolution EPR. We have compared the
binding configuration in the presence of quinone with the known
structures for the complex with stigmatellin and myxothiazol. We have
shown by using EPR and orientation-selective electron spin echo
envelope modulation (ESEEM) measurements of the iron-sulfur protein
that when quinone is present in the site, the isotropic hyperfine
constant of one of the N
ACCELERATED PUBLICATION
The Interaction of the Rieske Iron-Sulfur Protein with Occupants
of the Qo-site of the bc1 Complex,
Probed by Electron Spin Echo Envelope Modulation*
,
,**
Institute of Chemical Kinetics and
Combustion, Russian Academy of Sciences, Novosibirsk 630090, Russia,
the § Department of Biochemistry, University of Illinois,
Urbana, Illinois 61801, the ¶ Division of Natural Science, Osaka
Kyoiku University, Osaka 582-8582, Japan, the Department of
Biochemistry and Molecular Biology, Nippon Medical School, Tokyo
113-8062, Japan, and the ** Illinois EPR Research Center and
Department of Veterinary Clinical Medicine, University of Illinois,
Urbana, Illinois 61801
atoms of a liganding histidine
of the [2Fe-2S] cluster is similar to that observed when stigmatellin
is present and different from the configuration in the presence of
myxothiazol. The spectra also show complementary differences in
nitrogen quadrupole splittings in some orientations. We suggest that
the EPR characteristics, the ESEEM spectra, and the hyperfine couplings
reflect a similar interaction between the iron-sulfur protein and the
quinone or stigmatellin and that the N involved is that
of a histidine (equivalent to His-161 in the chicken mitochondrial
complex) that forms both a ligand to the cluster and a hydrogen
bond with a carbonyl oxygen atom of the Qo-site occupant.
*
This work was supported by National Institutes of Health
Grant GM35438 (to A. R. C.); NATO Grant 977132 (to A. R. C. and R. S.); National Science Foundation Grant
DBI-9602240 (to D. K.); National Science Foundation Grant
INT-9910113 (to S. A. D.); Ministry of Education, Science,
Sport and Culture of Japan Grant-in-aid 1169237, and Japan-United
States Cooperative Science Program Grant from JSPS BSAR-507 (to T. I.).The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported by Illinois EPR Research Center (National Institutes
of Health Grant RR01811). To whom correspondence should be addressed:
Illinois EPR Research Center, University of Illinois, Urbana, IL 61801. E-mail: dikanov@uiuc.edu.
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