5TDS

Toluene bound in the resting active site of toluene 4-monooxygenase (T4moH)

5TDS の概要

• エントリーDOI: 10.2210/pdb5tds/pdb
• 関連するPDBエントリー: 5TDT 5TDU 5TDV
• 分子名称: Toluene-4-monooxygenase system protein A, Toluene-4-monooxygenase system protein E, Toluene-4-monooxygenase system protein B, ... (8 entities in total)
• 機能のキーワード: diiron, hydroxylase, substrate complex, oxidoreductase
• 由来する生物種: Pseudomonas mendocina; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 212282.20

構造登録者

Acheson, J.F.,Fox, B.G. (登録日: 2016-09-19, 公開日: 2017-03-22, 最終更新日: 2023-10-04)

主引用文献

Acheson, J.F.,Bailey, L.J.,Brunold, T.C.,Fox, B.G.
In-crystal reaction cycle of a toluene-bound diiron hydroxylase.
Nature, 544:191-195, 2017

PubMed Abstract: Electrophilic aromatic substitution is one of the most important and recognizable classes of organic chemical transformation. Enzymes create the strong electrophiles that are needed for these highly energetic reactions by using O, electrons, and metals or other cofactors. Although the nature of the oxidants that carry out electrophilic aromatic substitution has been deduced from many approaches, it has been difficult to determine their structures. Here we show the structure of a diiron hydroxylase intermediate formed during a reaction with toluene. Density functional theory geometry optimizations of an active site model reveal that the intermediate is an arylperoxo Fe/Fe species with delocalized aryl radical character. The structure suggests that a carboxylate ligand of the diiron centre may trigger homolytic cleavage of the O-O bond by transferring a proton from a metal-bound water. Our work provides the spatial and electronic constraints needed to propose a comprehensive mechanism for diiron enzyme arene hydroxylation that accounts for many prior experimental results.

PubMed: 28346937
DOI: 10.1038/nature21681

実験手法

X-RAY DIFFRACTION (1.719 Å)