4683-50-5Relevant articles and documents
Catalyst-controlled regiodivergent vinylogous aza-Morita–Baylis–Hillman reactions
Hyakutake, Ryuichi,Gondo, Naruhiro,Ueda, Yoshihiro,Yoshimura, Tomoyuki,Furuta, Takumi,Kawabata, Takeo
supporting information, p. 1321 - 1324 (2018/03/29)
Regiodivergent vinylogous aza-Morita–Baylis–Hillman reactions of 3-vinylcyclopent-2-en-1-one 1 were developed in a catalyst-controlled manner. While treatment of 1 with N-tosylarylaldimines 2 in the presence of DABCO gave the α-adducts as the sole regiois
Ionic liquid supported on magnetic nanoparticles as highly efficient and recyclable catalyst for the synthesis of β-keto enol ethers
Li, Pei-He,Li, Bao-Le,Hu, Hai-Chuan,Zhao, Xiao-Na,Zhang, Zhan-Hui
, p. 118 - 122 (2014/01/17)
A magnetically ionic liquid supported on γ-Fe2O 3 nanocatalyst (AlxCly-IL-SiO 2γ-Fe2O3) was synthesized and evaluated as a recoverable catalyst for the synthesis of β-keto enol ethers. The immobilized catalyst proved to be effective and provided the products in high to excellent yield at room temperature. Moreover, the catalyst could be easily recovered by magnetic separation and recycled for six times without significant loss of its catalytic activity.
Asymmetric synthesis of O-protected acyloins using enoate reductases: Stereochemical control through protecting group modification
Winkler, Christoph K.,Stueckler, Clemens,Mueller, Nicole J.,Pressnitz, Desiree,Faber, Kurt
supporting information; experimental part, p. 6354 - 6358 (2011/02/24)
O-Protected cyclic acyloins were obtained in nonracemic form through asymmetric bioreduction of α,β-unsaturated alkoxy ketones by using 11 different enoate reductases from the "Old Yellow Enzyme" family. The stereochemical outcome of the biotransformation could be switched by variation of the O-protecting group or by the ring size of the substrate, which allows access to both stereoisomers in up to >97 % ee Whereas α-alkoxy enones were readily accepted as substrates, β-analogs were not converted. Overall, α-alkoxy enones represent a novel type of substrate for flavin-dependent ene-reductases. Copyright