1492-49-5Relevant academic research and scientific papers
An efficient and odorless synthesis of thioethers using 2-[Bis(alkylthio)methylene]-3-oxo-N-o-tolylbutanamides as thiol equivalents
Yu, Haifeng
, p. 367 - 371 (2012/04/23)
Using 2-[bis(alkylthio)methylene]-3-oxo-N-o-tolylbutanamides 1 as odorless thiol equivalents, an efficient and odorless synthesis of thioethers has been developed. Promoted by NaOH in EtOH, the cleavage of 1 commences to generate thiolate anions, and the generated thiolate anions then react with halides to give various thioethers in good yield. It is noteworthy that only a very faint odor of thiols can be perceived during both the reaction and the workup. Using 2-[bis(alkylthio)methylene]-3-oxo-N-o-tolylbutanamides as odorless thiol equivalents, an efficient and odorless synthesis of thioethers has been developed. Promoted by NaOH in EtOH, the cleavage of 2-[bis(alkylthio)methylene] -3-oxo-N-o-tolylbutanamides commences to generate thiolate anions, and the generated thiolate anions then react with halides to give various thioethers in good yield. Copyright
Coupling of Proteolysis to ATP Hydrolysis upon Escherichia coli Lon Protease Functioning: II. 1 Hydrolysis of ATP and Activity of the Enzyme Peptide Hydrolase Sites
Mel'nikov,Tsirul'nikov,Rotanova
, p. 101 - 109 (2007/10/03)
The absence of direct correlation between the efficiency of functioning of ATPase and peptide hydrolase sites of Lon protease was revealed. It was shown that Lon protease is an allosteric enzyme, in which the catalytic activity of peptide hydrolase sites is provided by the binding of nucleotides, their magnesium complexes, and free magnesium ions in the enzyme ATPase sites. It was revealed that the ADP-Mg complex, an inhibitor of the native enzyme, is an activator of the Lon-K362Q (the Lon protease mutant in the ATPase site). Variants of functional contacts between different sites of the enzyme are considered. It was established that two ways of signal transduction from the ATPase sites to peptide hydrolase ones exist in the Lon protease oligomer - intra- and intersubunit ways. The enzyme ATPase sites are suggested to be located in the areas of the complementary surfaces of subunits. It is hypothesized that upon degradation of protein substrates by the E. coli Lon protease in vivo ATP hydrolysis acts as a factor of limitation of the enzyme degrading activity.
Rate and Equilibrium Constants for the Reaction of Thiolate Ions with Dibenzo-1,2-dithiin and Naphtho-1,2-dithiole 1,1-Dioxides
Boduszek, Bogdan,Kice, John L.
, p. 2055 - 2060 (2007/10/02)
In aqueous dioxane the cyclic thiosulfonate dibenzo-1,2-dithiin 1,1-dioxide (1) reacts rapidly with thiolate ions and undergoes opening of the thiosulfonate ring (eq 2), forming disulfide 3a.Acidification of solutions of 3a with carboxylic acid buffers of appropiate pH leads to facile reversal of ring-opening reaction and the quantitative regeneration of 1.Since this reversal of ring opening is not acid-catalyzed, it must take place via a simple intramolecular displacement of RS- by the sulfinate (SO2-) group present in 3a and is therefore the microscopic reverse of the ring-opening reaction.Rate constants have been determined for both ring opening (kRS) and reversal of ring opening (k-RS) for a series of alkanethiolates of varying pKa.From these data one may also calculate the equilibrium constant, Keq(=kRS/k-RS), for reaction of each thiolate with 1.From comparison of the log Keq's with previously determined equilibrium constants for reaction of cyanide and sulfite ions with 1 one obtains quantitative information on the thermodynamics of reactions of the type ArSSR + CN- = ArSCN + RS- and ArSSR + SO32- = ArSSO3- + RS- that should be of considerable value for predicting the magnitude of equilibrium constants for cyanide-disulfide and sulfite-disulfide equilibria.Plots of log Keq, log KRS, and log k-RS vs. the pKa of RSH reveal that βeq=1.25, βRS=0.26, and β-RS=-0.99.These β values show that the transition state for eq 2 is quite unsymmetrical, with a structure Δ-...S-SO2δ-> where the RS-S bond is only ca. 20percent formed.The βRS and β-RS values are compared with the β values for several other previously studied displacements involving disulfides.The reaction of naphthol-1,2-dithiole 1,1-dioxide (2) with thiolates behaves in a fashion analogous to that of the reaction of RS- with 1.Comparison of Keq, kRS, and k-RS for an equilibrium involving 2 and a thiolate with those for the corresponding thiolate reacting with 1 allows one to assess how a change from a six- to a five-membered thiosulfonate ring influences Keq, kRS, and k-RS.The major effects are that k-RS is much larger and Keq is considerably smaller.
