7EMM

Crystal structure of IrCp* immobilized apo-R52H-rHLFr

7EMM の概要

• エントリーDOI: 10.2210/pdb7emm/pdb
• 分子名称: Ferritin light chain, 1,2-ETHANEDIOL, SULFATE ION, ... (7 entities in total)
• 機能のキーワード: iron storage protein, ir binding, metal binding protein
• 由来する生物種: Equus caballus (Horse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21970.80

構造登録者

Taher, M.,Maity, B.,Nakane, T.,Abe, S.,Ueno, T.,Mazumdar, S. (登録日: 2021-04-14, 公開日: 2022-03-02, 最終更新日: 2023-11-29)

主引用文献

Taher, M.,Maity, B.,Nakane, T.,Abe, S.,Ueno, T.,Mazumdar, S.
Controlled Uptake of an Iridium Complex inside Engineered apo-Ferritin Nanocages: Study of Structure and Catalysis.
Angew.Chem.Int.Ed.Engl., 61:e202116623-e202116623, 2022

PubMed Abstract: The effect of the mutation at the core of the ferritin nanocage (apo-rHLFr) on the uptake of IrCp* has been investigated by structural and spectroscopic methods. Site-specific mutations of two polar residues viz., Asp38 and Arg52 were investigated. The uptake of IrCp* was increased by about 1.5-fold on mutation of Arg52 by His compared to the wild-type variant, while mutation of Asp38 by His had no effect on the uptake. All the variants of the Ir-embedded ferritin cages remained as stable as the wild-type analogue. These hybrid bio-nanocages of ferritin were found to efficiently catalyze transfer hydrogenation of various substituted acetophenones forming the corresponding chiral alcohols with up to 88 % conversion and 70 % enantioselectivity. An electron-withdrawing substituent on the reactant enhanced the Turnover frequency of the reaction. Molecular docking analyses suggested that the substrate binds in different orientations at the active site in different mutants of the nanocage.

PubMed: 35005820
DOI: 10.1002/anie.202116623

実験手法

X-RAY DIFFRACTION (1.25 Å)