23343-16-0Relevant academic research and scientific papers
Benzisothiazol-3-ones through a Metal-Free Intramolecular N–S Bond Formation
Yang, Ke,Zhang, Hao,Niu, Ben,Tang, Tiandi,Ge, Haibo
supporting information, p. 5520 - 5523 (2018/10/26)
The highly efficient synthesis of benzoisothiazol-3-ones from thiobenzamides has been described with good functional group compatibility and excellent yields. This work represents the first example of selectfluor-promoted N–S bond formation processes. This method provides a facile approach to access various important bioactive benzoisothiazol-3-ones.
Method used for preparing amides via catalysis of halogenated aromatic hydrocarbons, amines, and carbon monoxide carbonylation with precious metal
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Paragraph 0019; 0058; 0060, (2017/10/07)
The invention discloses a method used for preparing amides via catalysis of halogenated aromatic hydrocarbons, amines, and carbon monoxide carbonylation with precious metal. According to the method, palladium acetate and triphenyl phosphine are taken as catalysts; a super strong alkali system is composed of potassium hydroxide and dimethyl sulphoxide, p-benzoquinone is taken as an oxidizing agent, carbon monoxide gas is taken as a carbonyl source, aniline is taken as a solvent, iodobenzene is taken as a substrate, carbonylation of iodobenzene into azophenyl benzamide at room temperature under normal pressure is realized. The method is high in conversion rate; reaction conditions are mild; less environment pollution is caused; the method is beneficial for large scale industrialized production, and promising application prospect and economic benefits are achieved.
Redox regulation of protein tyrosine phosphatase 1B (PTP1B): Importance of steric and electronic effects on the unusual cyclization of the sulfenic acid intermediate to a sulfenyl amide
Sarma, Bani Kanta
, p. 410 - 419 (2013/10/22)
The redox regulation of protein tyrosine phosphatase 1B (PTP1B) via the unusual transformation of its sulfenic acid (PTP1B-SOH) to a cyclic sulfenyl amide intermediate is studied by using small molecule chemical models. These studies suggest that the sulfenic acids derived from the H2O 2-mediated reactions o-amido thiophenols do not efficiently cyclize to sulfenyl amides and the sulfenic acids produced in situ can be trapped by using methyl iodide. Theoretical calculations suggest that the most stable conformer of such sulfenic acids are stabilized by n O→σ* S-OH orbital interactions, which force the -OH group to adopt a position trans to the S· · ·O interaction, leading to an almost linear arrangement of the O· · ·S-O moiety and this may be the reason for the slow cyclization of such sulfenic acids to their corresponding sulfenyl amides. On the other hand, additional substituents at the 6-position of o-amido phenylsulfenic acids that can induce steric environment and alter the electronic properties around the sulfenic acid moiety by S· · ·N or S· · ·O nonbonded interactions destabilize the sulfenic acids by inducing strain in the molecule. This may lead to efficient the cyclization of such sulfenic acids. This model study suggests that the amino acid residues in the close proximity of the sulfenic acid moiety in PTP1B may play an important role in the cyclization of PTP1B-SOH to produce the corresponding sulfenyl amide.
A chemical model for redox regulation of protein tyrosine phosphatase 1B (PTP1B) activity
Sivaramakrishnan, Santhosh,Keerthi, Kripa,Gates, Kent S.
, p. 10830 - 10831 (2007/10/03)
Growing evidence indicates that endogenously produced hydrogen peroxide acts as a cellular signaling molecule that (among other things) can regulate the activity of some protein phosphatases. Recent X-ray crystallographic studies revealed an unexpected chemical transformation underlying the redox regulation of protein tyrosine phosphatase 1B, in which oxidative inactivation of the enzyme yields an intrastrand protein cross-link between the catalytic cysteine residue and its neighboring amide nitrogen. This work describes a small organic molecule that serves as an effective model for the redox-sensing assembly of functional groups at the active site of PTP1B. Findings obtained using this model system suggest that the oxidative transformation of PTP1B to its "crosslinked" inactive form can proceed directly via oxidation of the active-site cysteine to a sulfenic acid (RSOH). The remarkably facile nature of this protein cross-link-forming reaction, along with the widespread cellular occurrence of protein sulfenic acids generated via oxidation of cysteine residues, suggests that the type of oxidative protein cross-link formation first seen in the context of PTP1B represents a potentially general mechanism for redox "switching" of protein function. Thus, the chemistry characterized here could have broad relevance to both redox-regulated signal transduction and the toxic effects of oxidative stress. Copyright
Reactions of N-sulfenyl-1,2-benzisothiazolin-3-ones with nucleophiles
Bao, Ming,Shimizu, Masao,Shimada, Shigeru,Inoue, Jun'ichi,Konakahara, Takeo
, p. 11359 - 11366 (2007/10/03)
Reactions of N-[2-(alkoxycarbonyl)benzenesulfenyl]-1,2-benzisothiazolin-3- ones (1) with various nucleophiles were examined. Anions of active methylene compounds attacked the sulfur atoms of the sulfenyl moieties of 1 to afford sulfide compounds, while th
A Novel Route to 2-Substituted 1,2-Benzisothiazol-3(2H)-ones
Uchida, Yuzuru,Kozuka, Seizi
, p. 510 - 511 (2007/10/02)
2-Alkyl- and 2-aryl-1,2-benzisothiazol-3(2H)-ones were synthesized in high yields by the cyclization of 2-(methylsulphinyl)benzamides with thionyl chloride.
