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Science 12 June 1998:
Vol. 280. no. 5370, pp. 1723 - 1729
DOI: 10.1126/science.280.5370.1723
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Research Articles

Redox-Coupled Crystal Structural Changes in Bovine Heart Cytochrome c Oxidase

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

Crystal structures of bovine heart cytochrome c oxidase in the fully oxidized, fully reduced, azide-bound, and carbon monoxide-bound states were determined at 2.30, 2.35, 2.9, and 2.8 angstrom resolution, respectively. An aspartate residue apart from the O2 reduction site exchanges its effective accessibility to the matrix aqueous phase for one to the cytosolic phase concomitantly with a significant decrease in the pK of its carboxyl group, on reduction of the metal sites. The movement indicates the aspartate as the proton pumping site. A tyrosine acidified by a covalently linked imidazole nitrogen is a possible proton donor for the O2 reduction by the enzyme.

S. Yoshikawa, K. Shinzawa-Itoh, R. Nakashima, R. Yaono, and C. Peters Libeu are in the Department of Life Science, Himeji Institute of Technology and CREST, Japan Science and Technology Corporation (JST), Kamigohri Akoh, Hyogo 678-1297, Japan. E. Yamashita, N. Inoue, M. Yao, M. J. Fei, T. Mizushima, T. Tomizaki, and T. Tsukihara are at the Institute for Protein Research, Osaka University, 3-2 Yamada-oka, Suita 565-0871, Japan. H. Yamaguchi is at the Faculty of Science, Kwansei Gakuin University, Uegahara, Nishinomiya Hyogo 662, Japan.
*   To whom correspondence should be addressed.

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