1121-30-8Relevant articles and documents
Kinetics and mechanism of the formation and reactions of S-nitroso derivatives of some heterocyclic thiones
Amado,Blakelock,Holmes,Williams
, p. 441 - 447 (2001)
Rate and equilibrium measurements have been obtained for the nitrosation (using nitrous acid in dilute acid aqueous solution) of the following thione-thiol nitrogen heterocyclic species and for the decomposition reactions of the formed S-NO- io
Protein Folding Stability Changes across the Proteome Reveal Targets of Cu Toxicity in E. coli
Wiebelhaus, Nancy,Zaengle-Barone, Jacqueline M.,Hwang, Kevin K.,Franz, Katherine J.,Fitzgerald, Michael C.
, p. 214 - 224 (2021)
The ability of metal ionophores to induce cellular metal hyperaccumulation endows them with potent antimicrobial activity; however, the targets and mechanisms behind these outcomes are not well understood. This work describes the first utilization of proteome-wide measurements of protein folding stability in combination with protein expression level analysis to identify protein targets of copper, thereby providing new insight into ionophore-induced copper toxicity in E. coli. The protein folding stability analysis employed a one-pot protocol for pulse proteolysis (PP) in combination with a semi-tryptic peptide enrichment strategy for proteolysis procedures (STEPP) to generate stability profiles for proteins in cell lysates derived from E. coli exposed to copper with and without two ionophores, the antimicrobial agent pyrithione and its β-lactamase-activated prodrug, PcephPT. As part of this work, the above cell lysates were also subject to protein expression level analysis using conventional quantitative bottom-up proteomic methods. The protein folding stability and expression level profiles generated here enabled the effects of ionophore vs copper to be distinguished and revealed copper-driven stability changes in proteins involved in processes spanning metabolism, translation, and cell redox homeostasis. The 159 differentially stabilized proteins identified in this analysis were significantly more numerous (～3×) than the 53 proteins identified with differential expression levels. These results illustrate the unique information that protein stability measurements can provide to decipher metal-dependent processes in drug mode of action studies.
Chemistry of Mercaptopyridines and Related Ligands. Part 3. Novel Examples of Copper(II)-Tertiary Phosphine Complexes stabilized by 1-Hydroxypyridine-2-thione
Lobana, Tarlok S.,Bhatia, Paramjit K.
, p. 1407 - 1410 (2007/10/02)
reaction of 1-hydroxypyridine-2-thione (C5H5NOS) with copper(II) chloride dihydrate gave an insoluble dirty yellow compound of stoichiometry, 1 which is ESR active.Similar reaction with copper(II) bromide gave the ESR-active green compound 7.Reactions of 1 and 7 with tertiary phosphines gave mixed-ligand complexes of stoichiometry CuX(C5H4NOS)Ln , all of which are ESR active.The latter complexes represent the first novel examples of air- and moisture-stable copper(II)-tertiary phopshine complexes in which Cu(II) is bonded to one halogen, one oxygen, one sulfur and two phosphorus atoms.
