Thiazoles and benzothiazoles undergo regioselective C2-H chalcogenation via the sequence of thiazole C2-functionalization with phosphines to produce phosphonium salts which in turn react with S- and Se-centered nucleophiles to give products of C2-H chalcogenation and allow for recovery of the starting phosphine. The atom economical sequence proceeds under mild conditions and features broad scope for both the nucleophiles (electron-rich, electron-poor, sterically hindered thiols) and the various substituted benzothiazoles. The access to the substituted medicinally relevant C2-thio benzothiazoles also enables stereoselectivity improvements in the modified Julia olefinations.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1039/d0ob00684j | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Selective C-H chalcogenation of thiazoles via thiazol-2-yl-phosphonium salts.
Org Biomol Chem
July 2020
Institute of Organic Chemistry and Macromolecular Chemistry, Friedrich Schiller University Jena, Humboldtstr. 10, 07743 Jena, Germany.
Thiazoles and benzothiazoles undergo regioselective C2-H chalcogenation via the sequence of thiazole C2-functionalization with phosphines to produce phosphonium salts which in turn react with S- and Se-centered nucleophiles to give products of C2-H chalcogenation and allow for recovery of the starting phosphine. The atom economical sequence proceeds under mild conditions and features broad scope for both the nucleophiles (electron-rich, electron-poor, sterically hindered thiols) and the various substituted benzothiazoles. The access to the substituted medicinally relevant C2-thio benzothiazoles also enables stereoselectivity improvements in the modified Julia olefinations.
View Article and Find Full Text PDFKinetic mechanism of pyranose 2-oxidase from trametes multicolor.
Biochemistry
May 2009
Department of Biochemistry and Center for Excellence in Protein Structure and Function, Faculty of Science, Mahidol University, Bangkok 10400, Thailand.
Pyranose 2-oxidase (P2O) from Trametes multicolor is a flavoprotein oxidase that catalyzes the oxidation of aldopyranoses by molecular oxygen to yield the corresponding 2-keto-aldoses and hydrogen peroxide. P2O is the first enzyme in the class of flavoprotein oxidases, for which a C4a-hydroperoxy-flavin adenine dinucleotide (FAD) intermediate has been detected during the oxidative half-reaction. In this study, the reduction kinetics of P2O by d-glucose and 2-d-d-glucose at pH 7.
View Article and Find Full Text PDFThe crystal structure of the octamer [r(guauaca)dC]2 with six Watson-Crick base-pairs and two 3' overhang residues.
J Mol Biol
May 2000
Department of Chemistry and Biochemistry, Ohio State University, Columbus 43210, USA.
The crystal structure of an alternating RNA octamer, r(guauaca)dC (RNA bases are in lower case while the only DNA base is in upper case), with two 3' overhang residues one of them a terminal deoxycytosine and the other a ribose adenine, has been determined at 2.2 A resolution. The refined structure has an Rwork 18.
View Article and Find Full Text PDFNeither kcat. nor kcat./Km for five aryl alpha-D-glucopyranosides correlates with aglycone pKa, and isotope effects, described according to the convention used by Cleland [(1982) CRC Crit.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!