Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase

Science

Volumn 280, Issue 5370, 1998, Pages 1723-1729

  Yoshikawa, Shinya ^a   Shinzawa Itoh, Kyoko ^a   Nakashima, Ryosuke ^a   Yaono, Rieko ^a   Yamashita, Eiki ^b   Inoue, Noriko ^b   Yao, Min ^b   Fei, Ming Jie ^b   Libeu, Clare Peters ^a   Mizushima, Tsunehiro ^b   Yamaguchi, Hiroshi ^c   Tomizaki, Takashi ^b   Tsukihara, Tomitake ^b  

^a JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^b OSAKA UNIVERSITY   (Japan)

^c KWANSEI GAKUIN UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ASPARTIC ACID; AZIDE; CARBON MONOXIDE; CARBOXYL GROUP; CYTOCHROME C OXIDASE; HEME; HEMERYTHRIN; HISTIDINE; HYDROGEN; HYDROXIDE; IMIDAZOLE DERIVATIVE; MAGNESIUM; METAL; NITROGEN; OXYGEN; PROTON; PROTON PUMP; TYROSINE; WATER;

ARTICLE; CELL RESPIRATION; CONFORMATIONAL TRANSITION; COVALENT BOND; CRYSTAL STRUCTURE; DENSITY; ELECTRON TRANSPORT; ENZYME STRUCTURE; HEART; HUMAN; HYDROGEN BOND; MITOCHONDRIAL MEMBRANE; MODEL; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL;

ANIMALS; ASPARTIC ACID; AZIDES; BINDING SITES; CARBON MONOXIDE; CATTLE; COPPER; CRYSTALLOGRAPHY, X-RAY; ELECTRON TRANSPORT COMPLEX IV; HEME; HYDROGEN BONDING; HYDROGEN PEROXIDE; HYDROGEN-ION CONCENTRATION; LIGANDS; METALS; MODELS, CHEMICAL; MODELS, MOLECULAR; MYOCARDIUM; OXIDATION-REDUCTION; OXYGEN; PROTEIN CONFORMATION; PROTON PUMPS; TYROSINE;

EID: 18144447465     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.280.5370.1723     Document Type: Article

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40. 1/2}, were calculated at each stage of the density modification to monitor progress of the refinement. After the refinement of the phases by the density modification, the respective free R factors of DM and correlation coefficients converged to 0.279 and 0.907 for the oxidized form, 0.266 and 0.906 for the reduced form, 0.279 and 0.905 for the CO form, and 0.271 and 0.879 for the azide form. Coordinates have been deposited in the Protein Data Bank.
41. 1/2}, were calculated at each stage of the density modification to monitor progress of the refinement. After the refinement of the phases by the density modification, the respective free R factors of DM and correlation coefficients converged to 0.279 and 0.907 for the oxidized form, 0.266 and 0.906 for the reduced form, 0.279 and 0.905 for the CO form, and 0.271 and 0.879 for the azide form. Coordinates have been deposited in the Protein Data Bank.
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45. c) difference map.
46. c) difference map.
47. c) difference map.
48. We thank N. Sakabe and N. Watanabe for data collection with the Weissenberg camera and synchrotron radiation. Supported in part by Grants-in-Aid for Scientific Research on Priority Area (Molecular Science on the Specific Roles of Metal Ions in Biological Functions to S.Y.), and Grants-in-Aid for Scientific Research (grant 40068119 to S.Y. and 06558102, 06276102, and 05244102 to T. Tsukihara) from the Ministry of Education and Culture of Japan, and Grant-in-Aid for "Research for the Future" Program from the Japan Society for the Promotion of Science (JSPS-RFTF96L00503 to T. Tsukihara). This research was done with the approval of the Photon Factory Advisory Committee, and the National Laboratory for High Energy Physics, Japan (Proposal 91-050 and 94G-041). T. Tsukihara and S.Y. are members of the TARA project of Tsukuba University and senior visiting scientists of RIKEN.