247244-64-0Relevant academic research and scientific papers
Chloroperoxidase-Catalyzed Achmatowicz Rearrangements
Thiel, Daniel,Blume, Fabian,J?ger, Christina,Deska, Jan
, p. 2717 - 2725 (2018/05/14)
Chloroperoxidase from Caldariomyces fumago catalyzes the selective oxidation of furfuryl alcohols in an Achmatowicz-type ring expansion. In combination with glucose oxidase as oxygen-activating biocatalyst, a purely enzymatic, aerobic protocol for the synthesis of 6-hydroxypyranone building blocks is obtained. Thanks to an only modest stereochemical bias of the oxygenating heme protein, optically active alcohols of either configuration are converted without a significant mismatch opening up opportunities for enantioselective multienzymatic cascades. Balancing the oxidase-driven aerobic activation, extended enzyme half-lives and productive conversion of poorly soluble and slowly reacting substrates can be achieved with high yields of the six-membered O-heterocycles.
Kinetic resolution of 2-furylcarbinols using the Sharpless oxidation and its application to the synthesis of (5R,6S)-6-acetoxy-5-hexadecanolide
Kametani, Tetsuji,Tsubuki, Masayoshi,Tatsuzaki, Yoko,Honda, Toshio
, p. 2107 - 2110 (2007/10/02)
Kinetic resolution of 2-furylcarbinols employing 10 mol% of Ti(OiPr)4 in the presence of molecular sieves 3A under the Sharpless oxidation condition generally affords corresponding optically active 2-furylcarbinols in a range of 80-9
