9QNE

Streptavidin with a thiophenol cofactor as artificial hydrogen atom transferase

これはPDB形式変換不可エントリーです。

9QNE の概要

• エントリーDOI: 10.2210/pdb9qne/pdb
• 分子名称: Streptavidin, 5-[(3~{a}~{S},4~{S},6~{a}~{R})-2-oxidanylidene-1,3,3~{a},4,6,6~{a}-hexahydrothieno[3,4-d]imidazol-4-yl]-~{N}-(3-sulfanylphenyl)pentanamide, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: hydrogen atom transfer, thiophenol, streptavidin, transferase
• 由来する生物種: Streptomyces avidinii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17292.93

構造登録者

Zhang, K.,Ward, T.R. (登録日: 2025-03-24, 公開日: 2025-11-12, 最終更新日: 2025-11-26)

主引用文献

Cao, H.,Zhang, K.,Gorbachev, V.,Vornholt, T.,Yu, K.,Chen, D.,Ward, T.R.
An Asymmetric Hydrogen Atom Transferase with an Abiological Thiophenol Cofactor.
J.Am.Chem.Soc., 147:41600-41609, 2025

PubMed Abstract: Biocatalytic hydrogen atom transfer (HAT) holds the potential to help address some long-standing challenges in organic synthesis. Although several families of enzymes rely on cysteine to perform HAT, these enzymes are rather impractical for synthetic purposes. To circumvent possible side reactions associated with cysteinyl radicals, we report herein artificial hydrogen atom transferases (AHATases) with an abiological thiophenol cofactor, capitalizing on biotin-streptavidin technology. Chemogenetic optimization afforded an AHATase with good reactivity and high enantioselectivity (er up to 93:7) for the photoinduced radical hydroamination of alkenes. Crystal structures suggest that aromatic-sulfur interactions are key contributing factors to cofactor anchoring and enantioinduction. Mechanistic studies support H atom abstraction and donation processes, both of which are catalyzed by the AHATase. Our work highlights the synthetic potential of thiol-based biocatalytic HAT and expands the repertoire of HAT biocatalysis.

PubMed: 41182164
DOI: 10.1021/jacs.5c12516

実験手法

X-RAY DIFFRACTION (1.84 Å)