7VUW

Bovine heart cytochrome c oxidase in the cyanide-bound fully oxidized state at 50 K

7VUW の概要

• エントリーDOI: 10.2210/pdb7vuw/pdb
• 分子名称: Cytochrome c oxidase subunit 1, Cytochrome c oxidase subunit 7A1, mitochondrial, Cytochrome c oxidase subunit 7B, mitochondrial, ... (30 entities in total)
• 機能のキーワード: cytochrome c oxidase membrane protein respiratory complex heme protein, oxidoreductase
• 由来する生物種: Bos taurus (Bovine); 詳細
• タンパク質・核酸の鎖数: 26
• 化学式量合計: 456046.48

構造登録者

Shimada, A.,Tsukihara, T. (登録日: 2021-11-04, 公開日: 2022-11-16, 最終更新日: 2024-01-17)

主引用文献

Shimada, A.,Baba, J.,Nagao, S.,Shinzawa-Itoh, K.,Yamashita, E.,Muramoto, K.,Tsukihara, T.,Yoshikawa, S.
Crystallographic cyanide-probing for cytochrome c oxidase reveals structural bases suggesting that a putative proton transfer H-pathway pumps protons.
J.Biol.Chem., 299:105277-105277, 2023

PubMed Abstract: Cytochrome c oxidase (CcO) reduces O in the O-reduction site by sequential four-electron donations through the low-potential metal sites (Cu and Fe). Redox-coupled X-ray crystal structural changes have been identified at five distinct sites including Asp, Arg, Glu, the hydroxyfarnesyl ethyl group of heme a, and Ser, respectively. These sites interact with the putative proton-pumping H-pathway. However, the metal sites responsible for each structural change have not been identified, since these changes were detected as structural differences between the fully reduced and fully oxidized CcOs. Thus, the roles of these structural changes in the CcO function are yet to be revealed. X-ray crystal structures of cyanide-bound CcOs under various oxidation states showed that the O-reduction site controlled only the Ser-including site, while the low-potential metal sites induced the other changes. This finding indicates that these low-potential site-inducible structural changes are triggered by sequential electron-extraction from the low-potential sites by the O-reduction site and that each structural change is insensitive to the oxidation and ligand-binding states of the O-reduction site. Because the proton/electron coupling efficiency is constant (1:1), regardless of the reaction progress in the O-reduction site, the structural changes induced by the low-potential sites are assignable to those critically involved in the proton pumping, suggesting that the H-pathway, facilitating these low-potential site-inducible structural changes, pumps protons. Furthermore, a cyanide-bound CcO structure suggests that a hypoxia-inducible activator, Higd1a, activates the O-reduction site without influencing the electron transfer mechanism through the low-potential sites, kinetically confirming that the low-potential sites facilitate proton pump.

PubMed: 37742916
DOI: 10.1016/j.jbc.2023.105277

実験手法

X-RAY DIFFRACTION (1.6 Å)