The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 Å

Science

Volumn 272, Issue 5265, 1996, Pages 1136-1144

  Tsukihara, Tomitake ^a   Aoyama, Hiroshi ^a   Yamashita, Eiki ^a   Tomizaki, Takashi ^a   Yamaguchi, Hiroshi ^a   Shinzawa Itoh, Kyoko ^a   Nakashima, Ryosuke ^a   Yaono, Rieko ^a   Yoshikawa, Shinya ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

CHOLIC ACID; COPPER; CYTOCHROME C OXIDASE; HEART ENZYME; HEME; IMIDAZOLE; MAGNESIUM; PHOSPHATIDYLETHANOLAMINE; PHOSPHATIDYLGLYCEROL; WATER; ZINC;

ARTICLE; CATTLE; CRYSTAL STRUCTURE; ELECTRON TRANSPORT; ENZYME STRUCTURE; ENZYME SUBUNIT; HYDROGEN BOND; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; ANIMALS; CATTLE; CELL NUCLEUS; COPPER; CRYSTALLOGRAPHY, X-RAY; ELECTRON TRANSPORT; ELECTRON TRANSPORT COMPLEX IV; HEME; HYDROGEN BONDING; IRON; MEMBRANE PROTEINS; MITOCHONDRIA, HEART; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; MYOCARDIUM; NUCLEOTIDES; OXIDATION-REDUCTION; OXYGEN; PHOSPHOLIPIDS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTON PUMPS; WATER;

EID: 0029942862     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.272.5265.1136     Document Type: Article

References (34)

1. B. G. Malmström, Chem. Rev. 90, 1247 (1990); G. T. Babcock and M. Wikström, Nature 356, 301 (1992).
2. B. G. Malmström, Chem. Rev. 90, 1247 (1990); G. T. Babcock and M. Wikström, Nature 356, 301 (1992).
3. We follow the terminology of Kadenbach for the subunits of cytochrome c oxidase [B. Kadenbach and P. Merle, FEBS Lett. 135, 1 (1981); B. Kadenbach, U. Ungibaver, J. Jaraush, U. Buge, L. Kuhn-Neutwig, Trends Biochem. Sci. 8, 398 (1983)].
4. We follow the terminology of Kadenbach for the subunits of cytochrome c oxidase [B. Kadenbach and P. Merle, FEBS Lett. 135, 1 (1981); B. Kadenbach, U. Ungibaver, J. Jaraush, U. Buge, L. Kuhn-Neutwig, Trends Biochem. Sci. 8, 398 (1983)].
5. R. A. Capaldi, Annu. Rev. Biochem. 59, 569 (1990).
6. O. Warburg and E. Negelein, Biochem. Z. 214, 64 (1929).
7. R. M. Garavito and D. Picol, Methods 1, 57 (1990).
8. T. Tsukihara et al., Science 269, 1069 (1995).
9. S. Iwata, C. Ostermeier, B. Ludwig, H. Michel, Nature 376, 660 (1995).
10. M. Muller, N. Labonia, A. Azzi, Biochem. Biophys. Res. Commun. 154, 1260 (1988); M. Raitio, T. Jalli, M. Saraste, EMBO J. 6, 2825 (1987).
11. M. Muller, N. Labonia, A. Azzi, Biochem. Biophys. Res. Commun. 154, 1260 (1988); M. Raitio, T. Jalli, M. Saraste, EMBO J. 6, 2825 (1987).
12. A. C. Bloomev, J. N. Champress, G. Bricoqne, R. Staden, A. Klug, Nature 276, 362 (1978).
13. C. Chothia, M. Levitt, D. Richardson, Proc. Natl. Acad. Sci. U.S.A. 74, 4130 (1977).
14. W. H. Andy-Mark et al., Nature 367, 750 (1994).
15. T. Härd et al., Science 249, 157 (1990).
16. Y.-Z. Zhang, G. Ewart, R. A. Capaldi, Biochemistry 30, 3674 (1991).
17. D. N. Beratan, J. N. Onuchic, J. R. Winkler, H. B. Gray, Science 258, 1740 (1992).
18. B. C. Hill, J. Biol. Chem. 269, 2419 (1994).
19. G. A. Palmer, Ed., Long Range Electron Transfer in Biology (Dekker, New York, 1991).
20. M. K. F. Wikström, H. J. Harman, W. J. Ingledew, B. Chance, FEBS Lett. 65, 259 (1976).
21. S. Yoshikawa and W. S. Caughey, J. Biol. Chem. 257, 412 (1982).
22. J. E. Morgan, M. I. Verkhovsky, M. Wikström, J. Bioenerg. Biomembr. 26, 599 (1994)
23. B. C. Wang, Methods Enzymol. 115, 90 (1985).
24. N. C. Robinson, Biochemistry 21, 184 (1982).
25. A. O. Vassilev, N. Plesofsky-Vig, R. Brambel. Proc. Natl. Acad. Sci. U.S.A. 92, 8680 (1995).
26. G. Anthony, A. Reiman, B. Kadenbach, ibid. 90, 1652 (1993).
27. 91 is expected from the mutagenesis results.
28. 91 is expected from the mutagenesis results.
29. 91 is expected from the mutagenesis results.
30. M. F. Perutz, Mechanism of Cooperativity and Allosteric Regulation in Proteins (Cambridge Univ. Press, Cambridge, 1990).
31. W. S. Caughey, H. Shimada, M. G. Choc, M. P. Tucker, Proc. Natl. Acad. Sci. U.S.A. 78, 2903 (1981); W. T. Potter, J. H. Hazzard, M. G. Choc, M. P. Tucker, W. S. Caughey, Biochemistry 29, 6283 (1990).
32. W. S. Caughey, H. Shimada, M. G. Choc, M. P. Tucker, Proc. Natl. Acad. Sci. U.S.A. 78, 2903 (1981); W. T. Potter, J. H. Hazzard, M. G. Choc, M. P. Tucker, W. S. Caughey, Biochemistry 29, 6283 (1990).
33. A. Brünger, J. Kuriyan, M. Karplus, Science 235, 458 (1987).
34. Supported in part by Grants-in-Aid for Scientific Research on Priority Area from the Ministry of Education and Culture of Japan [Bioinorganic Chemistry and Cell Energetics (S.Y.), and grants 06276102 and 05244102 (T.T.), Grant-in-Aid (06558102 to T.T.)] and from the New Energy and Industrial Technology Development Organization of Japan [Grant-in-Aid for the Proposal-Based Advanced Industrial Technology R&D Program (B-021 to S.Y.)]. The project was done with the approval of the Photon Factory Advisory Committee, and the National Laboratory for High Energy Physics, Japan (Proposal number 91-050 and 94G-041). We thank N. Sakabe, A. Nakagawa, N. Watanabe, and S. Ikemizu for assisting in data collection with the Weissenberg camera and synchrotron radiation.