6UFF
Structure of Ene-reductase 1 NostocER1 from cyanobacteria
Summary for 6UFF
| Entry DOI | 10.2210/pdb6uff/pdb |
| Descriptor | Ene-reductase 1, FLAVIN MONONUCLEOTIDE, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | oxidoreductase, ene reductase, cyanobacteria, alkene reductase |
| Biological source | Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) |
| Total number of polymer chains | 8 |
| Total formula weight | 364267.75 |
| Authors | Sandoval, B.,Jeffrey, P.D.,Hyster, T. (deposition date: 2019-09-24, release date: 2020-03-25, Last modification date: 2023-10-11) |
| Primary citation | 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 Cited by 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: 32181943DOI: 10.1002/anie.202003125 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.007 Å) |
Structure validation
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