3ASO

Bovine heart cytochrome C oxidase in the fully oxidized state measured at 0.9 angstrom wavelength

3ASO の概要

• エントリーDOI: 10.2210/pdb3aso/pdb
• 関連するPDBエントリー: 1OCC 1OCO 1OCR 1OCZ 1V54 1V55 2DYR 2DYS 2EIJ 2EIK 2EIL 2EIM 2EIN 2OCC 2ZXW 3ABK 3ABL 3ABM 3AG1 3AG2 3AG3 3AG4 3ASN
• 分子名称: Cytochrome c oxidase subunit 1, Cytochrome c oxidase subunit 7A1, Cytochrome c oxidase subunit 7B, ... (28 entities in total)
• 機能のキーワード: oxidoreductase
• 由来する生物種: Bos taurus (bovine); 詳細
• 細胞内の位置: Mitochondrion inner membrane; Multi-pass membrane protein: P00396 P68530 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: 441790.87

構造登録者

Suga, M.,Yano, N.,Muramoto, K.,Shinzawa-Itoh, K.,Maeda, T.,Yamashita, E.,Tsukihara, T.,Yoshikawa, S. (登録日: 2010-12-17, 公開日: 2011-08-03, 最終更新日: 2023-11-01)

主引用文献

Suga, M.,Yano, N.,Muramoto, K.,Shinzawa-Itoh, K.,Maeda, T.,Yamashita, E.,Tsukihara, T.,Yoshikawa, S.
Distinguishing between Cl- and O2(2-) as the bridging element between Fe3+ and Cu2+ in resting-oxidized cytochrome c oxidase
Acta Crystallogr.,Sect.D, 67:742-744, 2011

PubMed Abstract: Fully oxidized cytochrome c oxidase (CcO) under enzymatic turnover is capable of pumping protons, while fully oxidized CcO as isolated is not able to do so upon one-electron reduction. The functional difference is expected to be a consequence of structural differences: [Fe(3+)-OH(-)] under enzymatic turnover versus [Fe(3+)-O(2)(2-)-Cu(2+)] for the as-isolated CcO. However, the electron density for O(2)(2-) is equally assignable to Cl(-). An anomalous dispersion analysis was performed in order to conclusively demonstrate the absence of Cl(-) between the Fe(3+) and Cu(2+). Thus, the peroxide moiety receives electron equivalents from cytochrome c without affecting the oxidation states of the metal sites. The metal-site reduction is coupled to the proton pump.

PubMed: 21795816
DOI: 10.1107/S0907444911022803

実験手法

X-RAY DIFFRACTION (2.3 Å)