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

American Association for the Advancement of Science (AAAS) - Tập 272 Số 5265 - Trang 1136-1144 - 1996
Tomitake Tsukihara1, Hiroshi Aoyama1, Eiki Yamashita1, Takashi Tomizaki1, Hiroshi Yamaguchi1, Kyoko Shinzawa‐Itoh2, Ryosuke Nakashima2, Rieko Yaono2, Shinya Yoshikawa2
1T. Tsukihara, H. Aoyama, E. Yamashita, T. Tomizaki, H. Yamaguchi are at the Institute for Protein Research, Osaka University, 3-2 Yamada-oka, Suita 565, Japan.
2K. Shinzawa-Itoh, R. Nakashima, R. Yaono, S. Yoshikawa are at the Department of Life Science, Himeji Institute of Technology, Kamigohri Akoh, Hyogo 678-12, Japan.

Tóm tắt

The crystal structure of bovine heart cytochrome c oxidase at 2.8 Å resolution with an R value of 19.9 percent reveals 13 subunits, each different from the other, five phosphatidyl ethanolamines, three phosphatidyl glycerols and two cholates, two hemes A, and three copper, one magnesium, and one zinc. Of 3606 amino acid residues in the dimer, 3560 have been converged to a reasonable structure by refinement. A hydrogen-bonded system, including a propionate of a heme A (heme a), part of peptide backbone, and an imidazole ligand of Cu A , could provide an electron transfer pathway between Cu A and heme a. Two possible proton pathways for pumping, each spanning from the matrix to the cytosolic surfaces, were identified, including hydrogen bonds, internal cavities likely to contain water molecules, and structures that could form hydrogen bonds with small possible conformational change of amino acid side chains. Possible channels for chemical protons to produce H 2 O, for removing the produced water, and for O 2 , respectively, were identified.

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American Association for the Advancement of Science (AAAS)

Tập 272 Số 5265

1136-1144

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