Summary for 7TNB
| Entry DOI | 10.2210/pdb7tnb/pdb |
| Descriptor | NADH:flavin oxidoreductase/NADH oxidase, SULFATE ION, ACETATE ION, ... (5 entities in total) |
| Functional Keywords | reductase, oxidoreductase |
| Biological source | Caulobacter segnis |
| Total number of polymer chains | 1 |
| Total formula weight | 40569.86 |
| Authors | Garfinkle, S.E.,Jeffrey, P.,Hyster, T.K. (deposition date: 2022-01-20, release date: 2022-08-24, Last modification date: 2023-10-18) |
| Primary citation | Fu, H.,Cao, J.,Qiao, T.,Qi, Y.,Charnock, S.J.,Garfinkle, S.,Hyster, T.K. An asymmetric sp 3 -sp 3 cross-electrophile coupling using 'ene'-reductases. Nature, 610:302-307, 2022 Cited by PubMed Abstract: The catalytic asymmetric construction of Csp-Csp bonds remains one of the foremost challenges in organic synthesis. Metal-catalysed cross-electrophile couplings (XECs) have emerged as a powerful tool for C-C bond formation. However, coupling two distinct Csp electrophiles with high cross-selectivity and stereoselectivity continues as an unmet challenge. Here we report a highly chemoselective and enantioselective Csp-Csp XEC between alkyl halides and nitroalkanes catalysed by flavin-dependent 'ene'-reductases (EREDs). Photoexcitation of the enzyme-templated charge-transfer complex between an alkyl halide and a flavin cofactor enables the chemoselective reduction of alkyl halide over the thermodynamically favoured nitroalkane partner. The key C-C bond-forming step occurs by means of the reaction of an alkyl radical with an in situ-generated nitronate to form a nitro radical anion that collapses to form nitrite and an alkyl radical. An enzyme-controlled hydrogen atom transfer (HAT) affords high levels of enantioselectivity. This reactivity is unknown in small-molecule catalysis and highlights the potential for enzymes to use new mechanisms to address long-standing synthetic challenges. PubMed: 35952713DOI: 10.1038/s41586-022-05167-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.79 Å) |
Structure validation
Download full validation report
