1279694-04-0Relevant articles and documents
Trapping Reactions of the Sulfenyl and Sulfinyl Tautomers of Sulfenic Acids
Kumar, Murugaeson R.,Farmer, Patrick J.
, p. 474 - 478 (2017)
Sulfenic acids react as both nucleophiles and electrophiles, which may be attributable to interconversion between sulfenyl and sulfinyl tautomers. We demonstrate one-pot trapping of both tautomeric forms of glutathione sulfenic acid by LCMS. The sulfinyl
Nitrite reduction mediated by heme models. Routes to NO and HNO?
Heinecke, Julie L.,Khin, Chosu,Pereira, Jose Clayston Melo,Suárez, Sebastián A.,Iretskii, Alexei V.,Doctorovich, Fabio,Ford, Peter C.
, p. 4007 - 4017 (2013/04/23)
The water-soluble ferriheme model FeIII(TPPS) mediates oxygen atom transfer from inorganic nitrite to a water-soluble phosphine (tppts), dimethyl sulfide, and the biological thiols cysteine (CysSH) and glutathione (GSH). The products with the latter reductant are the respective sulfenic acids CysS(O)H and GS(O)H, although these reactive intermediates are rapidly trapped by reaction with excess thiol. The nitrosyl complex FeII(TPPS)(NO) is the dominant iron species while excess substrate is present. However, in slightly acidic media (pH ≈ 6), the system does not terminate at this very stable ferrous nitrosyl. Instead, it displays a matrix of redox transformations linking spontaneous regeneration of FeIII(TPPS) to the formation of both N2O and NO. Electrochemical sensor and trapping experiments demonstrate that HNO (nitroxyl) is formed, at least when tppts is the reductant. HNO is the likely predecessor of the N2O. A key pathway to NO formation is nitrite reduction by FeII(TPPS), and the kinetics of this iron-mediated transformation are described. Given that inorganic nitrite has protective roles during ischemia/reperfusion (I/R) injury to organs, attributed in part to NO formation, and that HNO may also reduce net damage from I/R, the present studies are relevant to potential mechanisms of such nitrite protection.
Quantification of protein sulfenic acid modifications using isotope-coded dimedone and iododimedone
Seo, Young Ho,Carroll, Kate S.
supporting information; experimental part, p. 1342 - 1345 (2011/04/22)
Quantitative proteomics: The new technique mentioned in the title-in short, ICDID-enables quantification of sulfenic acid modifications in proteins (see picture). The approach permits S-hydroxylation site occupancy to be monitored at individual cysteines
Formation of cysteine sulfenic acid by oxygen atom transfer from nitrite
Heinecke, Julie,Ford, Peter C.
body text, p. 9240 - 9243 (2010/11/02)
Cysteine sulfenic acid CysS(O)H is shown to be formed for the reaction of cysteine (CysSH) with aqueous nitrite and the water-soluble ferriheme models FeIII(TPPS) (TPPS = mesotetra(4-sulfonatophenyl)porphyrinato) or FeIII(TMPS) (TMPS = meso-tetra(sulfonatomesityl)porphyrinato) at pH 5.8 and 7.4. The other product is the respective ferrous nitrosyl complex FeII-(Por)(NO) (Por = TPPS or TMPS). Analogous oxygen atom transfers (OAT) were seen when glutathione (GSH) was used as the substrate. The sulfenic acids, CysS(O)H and GS(O)H, are transient species since they react rapidly with excess thiol to give the respective disulfides, so their presence as reactive intermediates was demonstrated by trapping with dimedone and detecting the resulting adduct using LC/MS. Preliminary kinetics studies are consistent with rate-limiting OAT from a ferric nitro complex FeIII(Por)(NO 2-) to CysSH, although this reaction is complicated by a competing dead-end equilibrium to form the thiolate complex (Fe III(TPPS)(CysS-).
