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Science 25 August 1995:
Vol. 269. no. 5227, pp. 1069 - 1074
DOI: 10.1126/science.7652554
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Articles

Science, Vol 269, Issue 5227, 1069-1074
Copyright © 1995 by American Association for the Advancement of Science

articles

Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 A

T Tsukihara, H Aoyama, E Yamashita, T Tomizaki, H Yamaguchi, K Shinzawa-Itoh, R Nakashima, R Yaono, and S Yoshikawa

Institute for Protein Research, Osaka University, Suita, Japan.

The high resolution three-dimensional x-ray structure of the metal sites of bovine heart cytochrome c oxidase is reported. Cytochrome c oxidase is the largest membrane protein yet crystallized and analyzed at atomic resolution. Electron density distribution of the oxidized bovine cytochrome c oxidase at 2.8 A resolution indicates a dinuclear copper center with an unexpected structure similar to a [2Fe-2S]-type iron-sulfur center. Previously predicted zinc and magnesium sites have been located, the former bound by a nuclear encoded subunit on the matrix side of the membrane, and the latter situated between heme a3 and CuA, at the interface of subunits I and II. The O2 binding site contains heme a3 iron and copper atoms (CuB) with an interatomic distance of 4.5 A; there is no detectable bridging ligand between iron and copper atoms in spite of a strong antiferromagnetic coupling between them. A hydrogen bond is present between a hydroxyl group of the hydroxyfarnesylethyl side chain of heme a3 and an OH of a tyrosine. The tyrosine phenol plane is immediately adjacent and perpendicular to an imidazole group bonded to CuB, suggesting a possible role in intramolecular electron transfer or conformational control, the latter of which could induce the redox-coupled proton pumping. A phenyl group located halfway between a pyrrole plane of the heme a3 and an imidazole plane liganded to the other heme (heme a) could also influence electron transfer or conformational control.


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Internal Electron Transfer in Cu-Heme Oxidases. THERMODYNAMIC OR KINETIC CONTROL?.
M. Brunori, A. Giuffre, E. D'Itri, and P. Sarti (1997)
J. Biol. Chem. 272, 19870-19874
   Abstract »    Full Text »    PDF »
Copper-mediated repression of the activation domain in the yeast Mac1p transcription factor.
J. A. Graden and D. R. Winge (1997)
PNAS 94, 5550-5555
   Abstract »    Full Text »    PDF »
The Archaeal SoxABCD Complex Is a Proton Pump in Sulfolobus acidocaldarius.
M. Gleissner, U. Kaiser, E. Antonopoulos, and G. Schafer (1997)
J. Biol. Chem. 272, 8417-8426
   Abstract »    Full Text »    PDF »
Q-band Electron Nuclear Double Resonance (ENDOR) and X-band EPR of the Sulfobetaine 12Heat-treated Cytochrome c Oxidase Complex.
S. M. Musser, Y.-C. Fann, R. J. Gurbiel, B. M. Hoffman, and S. I. Chan (1997)
J. Biol. Chem. 272, 203-209
   Abstract »    Full Text »    PDF »
On the Mechanism of Inhibition of Cytochrome c Oxidase by Nitric Oxide.
A. Giuffre, P. Sarti, E. D'Itri, G. Buse, T. Soulimane, and M. Brunori (1996)
J. Biol. Chem. 271, 33404-33408
   Abstract »    Full Text »    PDF »
Lipidic cubic phases: A novel concept for the crystallization of membrane proteins.
E. M. Landau and J. P. Rosenbusch (1996)
PNAS 93, 14532-14535
   Abstract »    Full Text »    PDF »
Probing Substrate Binding Site of the Escherichia coli Quinol Oxidases Using Synthetic Ubiquinol Analogues.
K. Sakamoto, H. Miyoshi, K. Takegami, T. Mogi, Y. Anraku, and H. Iwamura (1996)
J. Biol. Chem. 271, 29897-29902
   Abstract »    Full Text »    PDF »
SCO1 and SCO2 Act as High Copy Suppressors of a Mitochondrial Copper Recruitment Defect in Saccharomyces cerevisiae.
D. M. Glerum, A. Shtanko, and A. Tzagoloff (1996)
J. Biol. Chem. 271, 20531-20535
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Cloning and Characterization of PET100, a Gene Required for the Assembly of Yeast Cytochrome c Oxidase.
C. Church, C. Chapon, and R. O. Poyton (1996)
J. Biol. Chem. 271, 18499-18507
   Abstract »    Full Text »    PDF »
Probing a Role of Subunit IV of the Escherichia coli bo-type Ubiquinol Oxidase by Deletion and Cross-linking Analyses.
K. Saiki, H. Nakamura, T. Mogi, and Y. Anraku (1996)
J. Biol. Chem. 271, 15336-15340
   Abstract »    Full Text »    PDF »
The caa3 Terminal Oxidase of Bacillus stearothermophilus. TRANSIENT SPECTROSCOPY OF ELECTRON TRANSFER AND LIGAND BINDING.
A. Giuffre, E. D'Itri, S. Giannini, M. Brunori, T. Ubbink-Kok, W. N. Konings, and G. Antonini (1996)
J. Biol. Chem. 271, 13987-13992
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Characterization of COX17, a Yeast Gene Involved in Copper Metabolism and Assembly of Cytochrome Oxidase.
D. M. Glerum, A. Shtanko, and A. Tzagoloff (1996)
J. Biol. Chem. 271, 14504-14509
   Abstract »    Full Text »    PDF »
Modification of the pH Profile and Tetrabenazine Sensitivity of Rat VMAT1 by Replacement of Aspartate 404 with Glutamate.
S. Steiner-Mordoch, A. Shirvan, and S. Schuldiner (1996)
J. Biol. Chem. 271, 13048-13054
   Abstract »    Full Text »    PDF »


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