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Science 4 July 1997:
Vol. 277. no. 5322, pp. 60 - 66
DOI: 10.1126/science.277.5322.60
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Research Articles

Crystal Structure of the Cytochrome bc1 Complex from Bovine Heart Mitochondria

Di Xia, Chang-An Yu, Hoeon Kim, Jia-Zhi Xia, Anatoly M. Kachurin, Li Zhang, Linda Yu, Johann Deisenhofer *

On the basis of x-ray diffraction data to a resolution of 2.9 angstroms, atomic models of most protein components of the bovine cytochrome bc1 complex were built, including core 1, core 2, cytochrome b, subunit 6, subunit 7, a carboxyl-terminal fragment of cytochrome c1, and an amino-terminal fragment of the iron-sulfur protein. The positions of the four iron centers within the bc1 complex and the binding sites of the two specific respiratory inhibitors antimycin A and myxothiazol were identified. The membrane-spanning region of each bc1 complex monomer consists of 13 transmembrane helices, eight of which belong to cytochrome b. Closely interacting monomers are arranged as symmetric dimers and form cavities through which the inhibitor binding pockets can be accessed. The proteins core 1 and core 2 are structurally similar to each other and consist of two domains of roughly equal size and identical folding topology.

D. Xia, H. Kim, and J. Deisenhofer are in the Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75235, USA. C.-A. Yu, J.-Z. Xia, A. M. Kachurin, L. Zhang, and L. Yu are in the Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA.
*   To whom correspondence should be addressed. E-mail: jd{at}howie.swmed.edu

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K. Kojima, S. Kitada, K. Shimokata, T. Ogishima, and A. Ito (1998)
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H. Tian, L. Yu, M. W. Mather, and C.-A. Yu (1998)
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On the Mechanism of Quinol Oxidation in the bc1 Complex.
S. Junemann, P. Heathcote, and P. R. Rich (1998)
J. Biol. Chem. 273, 21603-21607
   Abstract »    Full Text »    PDF »
Activation of a Matrix Processing Peptidase from the Crystalline Cytochrome bc1 Complex of Bovine Heart Mitochondria.
K. Deng, L. Zhang, A. M. Kachurin, L. Yu, D. Xia, H. Kim, J. Deisenhofer, and C.-A. Yu (1998)
J. Biol. Chem. 273, 20752-20757
   Abstract »    Full Text »    PDF »
Interaction of 2-n-Heptyl-4-Hydroxyquinoline-N-Oxide with Dimethyl Sulfoxide Reductase of Escherichia coli.
Z. Zhao and J. H. Weiner (1998)
J. Biol. Chem. 273, 20758-20763
   Abstract »    Full Text »    PDF »
Structure-Function Relationships in OxlT, the Oxalate/Formate Transporter of Oxalobacter formigenes. TOPOLOGICAL FEATURES OF TRANSMEMBRANE HELIX 11 AS VISUALIZED BY SITE-DIRECTED FLUORESCENT LABELING.
D. Fu and P. C. Maloney (1998)
J. Biol. Chem. 273, 17962-17967
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Inhibitor binding changes domain mobility in the iron-sulfur protein of the mitochondrial bc1 complex from bovine heart.
H. Kim, D. Xia, C.-A. Yu, J.-Z. Xia, A. M. Kachurin, L. Zhang, L. Yu, and J. Deisenhofer (1998)
PNAS 95, 8026-8033
   Abstract »    Full Text »    PDF »
Complete Structure of the 11-Subunit Bovine Mitochondrial Cytochrome bc1 Complex.
S. Iwata, J. W. Lee, K. Okada, J. K. Lee, M. Iwata, B. Rasmussen, T. A. Link, S. Ramaswamy, and B. K. Jap (1998)
Science 281, 64-71
   Abstract »    Full Text »
New Insights into the Co-evolution of Cytochrome c Reductase and the Mitochondrial Processing Peptidase.
S. Brumme, V. Kruft, U. K. Schmitz, and H.-P. Braun (1998)
J. Biol. Chem. 273, 13143-13149
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The Role of Charged Amino Acids in the alpha 1-beta 4 Loop of the Iron-Sulfur Protein of the Cytochrome bc1 Complex of Yeast Mitochondria.
V. H. Obungu, Y. Wang, and D. S. Beattie (1998)
J. Biol. Chem. 273, 11917-11922
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Inhibitor Binding within the NarI Subunit (Cytochrome bnr) of Escherichia coli Nitrate Reductase A.
A. Magalon, R. A. Rothery, D. Lemesle-Meunier, C. Frixon, J. H. Weiner, and F. Blasco (1998)
J. Biol. Chem. 273, 10851-10856
   Abstract »    Full Text »    PDF »
Transmembrane heme delivery systems.
B. S. Goldman, D. L. Beck, E. M. Monika, and R. G. Kranz (1998)
PNAS 95, 5003-5008
   Abstract »    Full Text »    PDF »
Studies of the Cytochrome Subunits of Menaquinone:Cytochrome c Reductase (bc Complex) of Bacillus subtilis. EVIDENCE FOR THE COVALENT ATTACHMENT OF HEME TO THE CYTOCHROME b SUBUNIT.
J. Yu and N. E. Le Brun (1998)
J. Biol. Chem. 273, 8860-8866
   Abstract »    Full Text »    PDF »
Two Distinct and Independent Mitochondrial Targeting Signals Function in the Sorting of an Inner Membrane Protein, Cytochrome c1.
I. Arnold, H. Folsch, W. Neupert, and R. A. Stuart (1998)
J. Biol. Chem. 273, 1469-1476
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Molecular Genetic Identification of a Pathway for Heme Binding to Cytochrome b6.
R. Kuras, C. de Vitry, Y. Choquet, J. Girard-Bascou, D. Culler, S. Buschlen, S. Merchant, and F.-A. Wollman (1997)
J. Biol. Chem. 272, 32427-32435
   Abstract »    Full Text »    PDF »
The Involvement of Serine 175 and Alanine 185 of Cytochrome b of Rhodobacter sphaeroides Cytochrome bc1 Complex in Interaction with Iron-Sulfur Protein.
H. Tian, L. Yu, M. W. Mather, and C.-A. Yu (1997)
J. Biol. Chem. 272, 23722-23728
   Abstract »    Full Text »    PDF »


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