14621-84-2Relevant articles and documents
Van der Merwe et al.
, p. 3923 (1964)
Wright et al.
, p. 821,823 (1972)
Efficient, scalable and economical preparation of tris(deuterium)- and 13C-labelled N-methyl-N-nitroso-p-toluenesulfonamide (Diazald) and their conversion to labelled diazomethane
Shields, Samuel W.J.,Manthorpe, Jeffrey M.
, p. 674 - 679 (2015/01/16)
A method for the preparation of multi-gramme quantities of N-methyl-d3-N-nitroso-p-toluenesulfonamide (Diazald-d3) and N-methyl-13C-N-nitroso-p-toluenesulfonamide (Diazald-13C) and their conversion to diazomethane-d2 and diazomethane-13C, respectively, is presented. This approach uses robust and reliable chemistry, and critically, employs readily commercially available and inexpensivemethanol as the label source. Several reactions of labelled diazomethane are also reported, including alkene cyclopropanation, phenolmethylation and α-diazoketone formation, as well as deuteriumscrambling in the preparation of diazomethane-d2 and subsequent methyl esterification of benzoic acid.
Methyl Trideuteriomethyl (E)-(α-Bromoarylidene)malonates: Simple Stereochemical Probes in Nucleophilic Vinylic Substitution near the Retention/Stereoconvergence Borderline
Rappoport, Zvi,Gazit, Aviv
, p. 6698 - 6710 (2007/10/02)
Methyl trideuteriomethyl (E)-(α-bromo-p-methyl- and -p-nitrobenzylidene)malonates (4 and 5) were prepared.These electrophilic bromo olefins are activated to vinylic substitution by ywo chemically identical but isotopically distinguishable CO2Me groups.The
Stereochemical studies on the reactions catalyzed by the PLP-dependent enzyme 1-aminocyclopropane-1-carboxylate deaminase
Liu,Auchus,Walsh
, p. 5335 - 5348 (2007/10/07)
The stereochemical course of 1-aminocyclopropane-1-carboxylate deaminase which catalyzes the fragmentation of the cyclopropane substrate to alpha -ketobutyrate and ammonia has been unraveled with the help of substrates stereospecifically labeled with deuterium and/or tritium, and this has afforded important information about the process occurring at the active site during enzymatic conversion.