Redox-Coupled Crystal Structural Changes in Bovine Heart Cytochrome c Oxidase-Reference-Cited by-同舟云学术

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

Published:1998-06-12 Issue:5370 Volume:280 Page:1723-1729
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Yoshikawa Shinya¹,Shinzawa-Itoh Kyoko¹,Nakashima Ryosuke¹,Yaono Rieko¹,Yamashita Eiki¹,Inoue Noriko¹,Yao Min¹,Fei Ming Jie¹,Libeu Clare Peters¹,Mizushima Tsunehiro¹,Yamaguchi Hiroshi¹,Tomizaki Takashi¹,Tsukihara Tomitake¹

Affiliation:

1. 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,...

Abstract

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 O 2 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 O 2 reduction by the enzyme.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference39 articles.

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2. Structures of Metal Sites of Oxidized Bovine Heart Cytochrome c Oxidase at 2.8 Å

3. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans

4. The Whole Structure of the 13-Subunit Oxidized Cytochrome c Oxidase at 2.8 Å

5. Purification of the enzyme preparation with repeated recrystallization is the most critical for improvement of the crystallization conditions of this enzyme. The crystals of fully reduced and CO-bound fully reduced forms were prepared by soaking the crystals of fully oxidized form in the medium containing ascorbate and a catalytic amount of cytochrome c as a reducing system and polyethylene glycol (PEG 4000) for stabilizing crystals under N2 and CO atmosphere, respectively. X-ray diffraction experiments were performed on these forms by placing crystals in capillaries filled with the appropriate soaking media. The oxidation state and the ligand-binding state of the enzyme were confirmed by absorption spectra of these crystals taken under the same medium conditions. Azide form was prepared by soaking the crystals of fully oxidized form into the buffer containing azide and appropriate amount of PEG 4000 under aerobic conditions. Intensity data were collected with synchrotron radiation of 1.0 Å at the Photon Factory, Tsukuba, Japan, by means of a modified Weissenberg camera for macromolecules [Sakabe N., J. Appl. Crystallogr. 16, 542 (1983)].

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