36873-36-6Relevant articles and documents
Asymmetric Reductive Carbocyclization Using Engineered Ene Reductases
Heckenbichler, Kathrin,Schweiger, Anna,Brandner, Lea Alexandra,Binter, Alexandra,Toplak, Marina,Macheroux, Peter,Gruber, Karl,Breinbauer, Rolf
supporting information, p. 7240 - 7244 (2018/06/15)
Ene reductases from the Old Yellow Enzyme (OYE) family reduce the C=C double bond in α,β-unsaturated compounds bearing an electron-withdrawing group, for example, a carbonyl group. This asymmetric reduction has been exploited for biocatalysis. Going beyond its canonical function, we show that members of this enzyme family can also catalyze the formation of C?C bonds. α,β-Unsaturated aldehydes and ketones containing an additional electrophilic group undergo reductive cyclization. Mechanistically, the two-electron-reduced enzyme cofactor FMN delivers a hydride to generate an enolate intermediate, which reacts with the internal electrophile. Single-site replacement of a crucial Tyr residue with a non-protic Phe or Trp favored the cyclization over the natural reduction reaction. The new transformation enabled the enantioselective synthesis of chiral cyclopropanes in up to >99 % ee.
A biologically inspired CuI/topaquinone-like co-catalytic system for the highly atom-economical aerobic oxidation of primary amines to imines
Largeron, Martine,Fleury, Maurice-Bernard
body text, p. 5409 - 5412 (2012/06/18)
Acting together: Low catalytic amounts of CuI and topaquinone-like catalyst 1ox (see scheme) are sufficient to activate the α-C-H bond of primary amines, which are converted into alkylated imines under ambient conditions. This atom-economical process tolerates the presence of various reactive functional groups and allows selective cross-coupling of two amines. Copyright
