1191-43-1Relevant articles and documents
Catalytic Hydrogenation of Thioesters, Thiocarbamates, and Thioamides
Luo, Jie,Rauch, Michael,Avram, Liat,Ben-David, Yehoshoa,Milstein, David
supporting information, p. 21628 - 21633 (2021/01/11)
Direct hydrogenation of thioesters with H2 provides a facile and waste-free method to access alcohols and thiols. However, no report of this reaction is documented, possibly because of the incompatibility of the generated thiol with typical hydrogenation catalysts. Here, we report an efficient and selective hydrogenation of thioesters. The reaction is catalyzed by an acridine-based ruthenium complex without additives. Various thioesters were fully hydrogenated to the corresponding alcohols and thiols with excellent tolerance for amide, ester, and carboxylic acid groups. Thiocarbamates and thioamides also undergo hydrogenation under similar conditions, substantially extending the application of hydrogenation of organosulfur compounds.
Reduction of thiokols in the system hydrazine hydrate-base as a new route to alkanedithiols
Alekminskaya,Russavskaya,Korchevin,Deryagina,Trofimov
, p. 732 - 737 (2007/10/03)
A new procedure for preparative synthesis of alkanedithiols from simple commercially available products is based on reduction of the S-S bond in appropriate polyalkylene disulfides (thiokols) in the system hydrazine hydrate-base. Thiokols were prepared by reaction of dihaloalkanes with Na2S2 or K2S2 generated from elemental sulfur and alkali in aqueous hydrazine hydrate. Reaction of 1,2-dibromocyclohexane with sodium or potassium disulfide yields bis(2-bromocyclohexyl) sulfide as the only product.
A Reagent for Reduction of Disulfide Bonds in Proteins That Reduces Disulfide Bonds Faster Than Does Dithiothreitol
Singh, Rajeeva,Whitesides, George M.
, p. 2332 - 2337 (2007/10/02)
We have synthesized a new reagent - N,N'-dimethyl-N,N'-bis(mercaptoacetyl)hydrazine (DMH) - for the reduction of disulfide bonds in proteins.DMH reduces disulfide bonds 7 times faster than does dithiothreitol (DTT) in water at pH 7.DMH reduces mixed disulfides of cysteine proteases (papain and ficin) especially rapidly (30 times faster than DTT).DMH (ε0 = -0.300 V) reduces noncyclic disulfides completely, although it is less strongly reducing than DTT (ε0 = -0.356 V).