6PTT

Soluble model of Arabidopsis thaliana CuA (Tt3LAt)

6PTT の概要

• エントリーDOI: 10.2210/pdb6ptt/pdb
• 分子名称: Cytochrome c oxidase subunit 2, DINUCLEAR COPPER ION (3 entities in total)
• 機能のキーワード: cua site, electron transfer, cupredoxin fold, electron transport, oxidoreductase
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28398.10

構造登録者

Lisa, M.N.,Giannini, E.,Llases, M.E.,Alzari, P.M.,Vila, A.J. (登録日: 2019-07-16, 公開日: 2019-11-20, 最終更新日: 2023-10-11)

主引用文献

Morgada, M.N.,Llases, M.E.,Giannini, E.,Castro, M.A.,Alzari, P.M.,Murgida, D.H.,Lisa, M.N.,Vila, A.J.
Unexpected electron spin density on the axial methionine ligand in CuAsuggests its involvement in electron pathways.
Chem.Commun.(Camb.), 56:1223-1226, 2020

PubMed Abstract: The CuA center is a paradigm for the study of long-range biological electron transfer. This metal center is an essential cofactor for terminal oxidases like cytochrome c oxidase, the enzymatic complex responsible for cellular respiration in eukaryotes and in most bacteria. CuA acts as an electron hub by transferring electrons from reduced cytochrome c to the catalytic site of the enzyme where dioxygen reduction takes place. Different electron transfer pathways have been proposed involving a weak axial methionine ligand residue, conserved in all CuA sites. This hypothesis has been challenged by theoretical calculations indicating the lack of electron spin density in this ligand. Here we report an NMR study with selectively labeled methionine in a native CuA. NMR spectroscopy discloses the presence of net electron spin density in the methionine axial ligand in the two alternative ground states of this metal center. Similar spin delocalization observed on two second sphere mutants further supports this evidence. These data provide a novel view of the electronic structure of CuA centers and support previously neglected electron transfer pathways.

PubMed: 31897463
DOI: 10.1039/c9cc08883k

実験手法

X-RAY DIFFRACTION (1.84 Å)