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Science 3 July 1998: Vol. 281. no. 5373, pp. 64 - 71 DOI: 10.1126/science.281.5373.64
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Research Articles
Complete Structure of the 11-Subunit Bovine Mitochondrial Cytochrome bc1 Complex
So Iwata,
*
Joong W. Lee,
Kengo Okada,
John Kyongwon Lee,
Momi Iwata,
Bjarne Rasmussen,
Thomas A. Link,
S. Ramaswamy,
Bing K. Jap
*
Mitochondrial cytochrome bc1 complex
performs two functions: It is a respiratory multienzyme complex and it
recognizes a mitochondrial targeting presequence. Refined crystal
structures of the 11-subunit bc1 complex from
bovine heart reveal full views of this bifunctional enzyme. The
"Rieske" iron-sulfur protein subunit shows significant conformational changes in different crystal forms, suggesting a new
electron transport mechanism of the enzyme. The mitochondrial targeting
presequence of the "Rieske" protein (subunit 9) is lodged between
the two "core" subunits at the matrix side of the complex. These
"core" subunits are related to the matrix processing peptidase, and
the structure unveils how mitochondrial targeting presequences are
recognized.
J. W. Lee, J. K. Lee, and B. K. Jap are in the Life
Sciences Division, Lawrence Berkeley National Laboratory, University of
California, Berkeley, CA 94720, USA. S. Iwata, K. Okada, and M. Iwata
are in the Department of Biochemistry, Uppsala University, BMC, Box
, Uppsala S-75123, Sweden. S. Ramaswamy is in the Department of
Molecular Biology, Swedish Agricultural Science University, Box , Biomedical Center, Uppsala S-75124, Sweden. T. A. Link is at
Uniklinikum Frankfurt, ZBC, Biochemie I, Molecular Bioenergetics,
D-60590 Frankfurt/Main, Germany. B. Rasmussen is at the Grenoble
Outstation, European Molecular Biology Laboratory, c/o Institut
Laue-Langevin, Boîte Postale 156, F-38042 Grenoble Cedex 9, France.
*
To whom correspondence should be addressed. E-mail: BKJap{at}lbl.gov
(B.K.J.) or iwata{at}xray.bmc.uu.se (S.I.)
Present address: Nara Institute of Science and Technology,
Division of Structural Biology, Department of Molecular Biology, Graduate School of Biological Sciences, 8916-5 Takayama, Ikoma, Nara
630-0101, Japan.
Read the Full Text
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- Molecular Basis of Proton Motive Force Generation: Structure of Formate Dehydrogenase-N.
- M. Jormakka, S. Tornroth, B. Byrne, and S. Iwata (2002)
Science
295, 1863-1868
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- From the Cover: Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome c.
- C. Lange and C. Hunte (2002)
PNAS
99, 2800-2805
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- 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.
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J. Biol. Chem.
277, 4605-4608
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- C-terminal Periplasmic Domain of Escherichia coli Quinoprotein Glucose Dehydrogenase Transfers Electrons to Ubiquinone.
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J. Biol. Chem.
276, 48356-48361
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- Evidence for the Intertwined Dimer of the Cytochrome bc1 Complex in Solution.
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J. Biol. Chem.
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