6Y2T

Streptavidin wildtype with a biotC4-1 cofactor - an artificial iron hydroxylase

これはPDB形式変換不可エントリーです。

6Y2T の概要

• エントリーDOI: 10.2210/pdb6y2t/pdb
• 分子名称: Streptavidin, biotC4-1 cofactor, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: artificial metalloenzyme, iron hydroxylase, biotin-binding protein, oxidoreductase
• 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: 18088.33

構造登録者

Serrano-Plana, J.,Rumo, C.,Rebelein, J.G.,Peterson, R.L.,Barnet, M.,Ward, T.R. (登録日: 2020-02-17, 公開日: 2020-07-01, 最終更新日: 2024-01-24)

主引用文献

Serrano-Plana, J.,Rumo, C.,Rebelein, J.G.,Peterson, R.L.,Barnet, M.,Ward, T.R.
Enantioselective Hydroxylation of Benzylic C(sp3)-H Bonds by an Artificial Iron Hydroxylase Based on the Biotin-Streptavidin Technology.
J.Am.Chem.Soc., 142:10617-10623, 2020

PubMed Abstract: The selective hydroxylation of C-H bonds is of great interest to the synthetic community. Both homogeneous catalysts and enzymes offer complementary means to tackle this challenge. Herein, we show that biotinylated Fe(TAML)-complexes (TAML = Tetra Amido Macrocyclic Ligand) can be used as cofactors for incorporation into streptavidin to assemble artificial hydroxylases. Chemo-genetic optimization of both cofactor and streptavidin allowed optimizing the performance of the hydroxylase. Using HO as oxidant, up to ∼300 turnovers for the oxidation of benzylic C-H bonds were obtained. Upgrading the ee was achieved by kinetic resolution of the resulting benzylic alcohol to afford up to >98% ee for ()-tetralol. X-ray analysis of artificial hydroxylases highlights critical details of the second coordination sphere around the Fe(TAML) cofactor.

PubMed: 32450689
DOI: 10.1021/jacs.0c02788

実験手法

X-RAY DIFFRACTION (1.55 Å)