6UFF

Structure of Ene-reductase 1 NostocER1 from cyanobacteria

6UFF の概要

• エントリーDOI: 10.2210/pdb6uff/pdb
• 分子名称: Ene-reductase 1, FLAVIN MONONUCLEOTIDE, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: oxidoreductase, ene reductase, cyanobacteria, alkene reductase
• 由来する生物種: Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 364267.75

構造登録者

Sandoval, B.,Jeffrey, P.D.,Hyster, T. (登録日: 2019-09-24, 公開日: 2020-03-25, 最終更新日: 2023-10-11)

主引用文献

Nakano, Y.,Black, M.J.,Meichan, A.J.,Sandoval, B.A.,Chung, M.M.,Biegasiewicz, K.F.,Zhu, T.,Hyster, T.K.
Photoenzymatic Hydrogenation of Heteroaromatic Olefins Using 'Ene'-Reductases with Photoredox Catalysts.
Angew.Chem.Int.Ed.Engl., 59:10484-10488, 2020

PubMed Abstract: Flavin-dependent 'ene'-reductases (EREDs) are highly selective catalysts for the asymmetric reduction of activated alkenes. This function is, however, limited to enones, enoates, and nitroalkenes using the native hydride transfer mechanism. Here we demonstrate that EREDs can reduce vinyl pyridines when irradiated with visible light in the presence of a photoredox catalyst. Experimental evidence suggests the reaction proceeds via a radical mechanism where the vinyl pyridine is reduced to the corresponding neutral benzylic radical in solution. DFT calculations reveal this radical to be "dynamically stable", suggesting it is sufficiently long-lived to diffuse into the enzyme active site for stereoselective hydrogen atom transfer. This reduction mechanism is distinct from the native one, highlighting the opportunity to expand the synthetic capabilities of existing enzyme platforms by exploiting new mechanistic models.

PubMed: 32181943
DOI: 10.1002/anie.202003125

実験手法

X-RAY DIFFRACTION (2.007 Å)