2OCC

BOVINE HEART CYTOCHROME C OXIDASE AT THE FULLY OXIDIZED STATE

2OCC の概要

• エントリーDOI: 10.2210/pdb2occ/pdb
• 分子名称: CYTOCHROME C OXIDASE, COPPER (II) ION, MAGNESIUM ION, ... (19 entities in total)
• 機能のキーワード: oxidoreductase, cytochrome(c)-oxygen, cytochrome c oxidase
• 由来する生物種: Bos taurus (cattle); 詳細
• 細胞内の位置: Mitochondrion inner membrane; Multi-pass membrane protein: P00396 P00404 P00415; Mitochondrion inner membrane: P07470 P13183 P00430 P10175 P00423 P00426 P00428 P07471 P04038; Mitochondrion intermembrane space: P00429
• タンパク質・核酸の鎖数: 26
• 化学式量合計: 413719.25

構造登録者

Tsukihara, T.,Yao, M. (登録日: 1998-05-26, 公開日: 1999-01-13, 最終更新日: 2024-10-30)

主引用文献

Yoshikawa, S.,Shinzawa-Itoh, K.,Nakashima, R.,Yaono, R.,Yamashita, E.,Inoue, N.,Yao, M.,Fei, M.J.,Libeu, C.P.,Mizushima, T.,Yamaguchi, H.,Tomizaki, T.,Tsukihara, T.
Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase.
Science, 280:1723-1729, 1998

PubMed 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 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.

PubMed: 9624044
DOI: 10.1126/science.280.5370.1723

実験手法

X-RAY DIFFRACTION (2.3 Å)