Comparison of the reactivity of <i>N</i>‐(<i>p</i>‐toluenesulfonyl)‐sulfinimidoyl fluorides and chlorides toward triphenylphosphine

Pashinnik, V. E.; Borovikov, Alexei V.; Shermolovich, Yu. G.

doi:10.1002/hc.20408

Cited by 3 publications

(1 citation statement)

References 17 publications

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“…Irrespective of conditions, one of the products is difluorotriphenylphosphorane. 252 New synthetic applications of tertiary phosphine-positive halogen reagents include the use of a combination of triphenylphosphine, bromine and tetrabutylammonium nitrite for the synthesis of N-nitrosamines and azides from the corresponding amines and hydrazides at 0 1C to room temperature, 253 a simple and efficient protocol for the chlorination of Bayliss-Hillman adducts using the triphenylphosphine-carbon tetrachloride system, 254 and the use of a combination of trichloroacetonitrile, triphenylphosphine and sodium azide at room temperature for the direct synthesis of acyl azides from carboxylic acids. 255 A combination of trichloroacetamide and triphenylphosphine provides a versatile reagent for the synthesis of esters 256 and a combination of ethyl tribromoacetate and triphenylphosphine has been used for the synthesis of a-bromoacrylates from aldehydes.…”

Section: Bhmentioning

confidence: 99%

Phosphines and related C–P bonded compounds

Allen¹

2016

Organophosphorus Chemistry

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Section: Bhmentioning

confidence: 99%

Phosphines and related C–P bonded compounds

Allen¹

2016

Organophosphorus Chemistry

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Water-Soluble Triarylphosphines as Biomarkers for Protein S-Nitrosation

Bechtold

Reisz

Klomsiri³

et al. 2010

ACS Chem. Biol.

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S-Nitrosothiols (RSNOs) represent an important class of post-translational modifications that preserve and amplify the actions of nitric oxide and regulate enzyme activity. Several regulatory proteins are now verified targets of cellular S-nitrosation and the direct detection of S-nitrosated residues in proteins has become essential to better understand RSNO-mediated signaling. Current RSNO detection depends on indirect assays that limit their overall specificity and reliability. Herein, we report the reaction of S-nitrosated cysteine, glutathione, and a mutated C165S alkyl hydroperoxide reductase with the water-soluble phosphine, tris(4,6-dimethyl-3-sulfonatophenyl)phosphine trisodium salt hydrate (TXPTS). A combination of NMR and MS techniques reveals these reactions produce covalent S-alkylphosphonium ion adducts (with S-P + connectivity), TXPTS oxide and a TXPTS-derived aza-ylide. Mechanistically, this reaction may proceed through an S-substituted azaylide or the direct displacement of nitroxyl from the RSNO group. This work provides a new means for detecting and quantifying S-nitrosated species in solution and suggests that phosphines may be useful tools for understanding the complex physiological roles of S-nitrosation and its implications in cell signaling and homeostasis. KeywordsS-nitrosothiol; triarylphosphine; aza-ylide; S-alkylphosphonium ion; protein labeling; chemical ligation; nitrosative stress Reactive oxygen and nitrogen species (ROS/RNS) affect cellular signaling processes at concentrations far below those required to inflict oxidative damage (1-4). The over-oxidation and metabolism of nitric oxide (NO), an endogenous cell signaling agent, produces several RNS including nitrogen dioxide and nitrite, which can generate competent nitrosation agents (5,6). Nitrosation of cysteine sites yields S-nitrosothiols (RSNOs) that preserve, modulate, and amplify the actions of NO. This selective and reversible process represents an important postCorrespondence to: S. Bruce King, kingsb@wfu.edu. † Department of Chemistry ‡ Center for Structural Biology § Department of Molecular Medicine Supporting Information available: Experimental details for the synthesis of Cys-SNO, GSNO and AhpC-SNO. 31 P and 13 C NMR spectra, UV/vis data and LC-MS results for various reactions. ESI-TOF-MS controls and x-ray structural data for 1. This material is available free of charge via the Internet at http://pubs.acs.org. (3,(6)(7)(8). Several proteins have been identified as targets of cellular S-nitrosation including glyceraldehyde-3-phosphate dehydrogenase (GAPDH), papain, hemoglobin (Hb), and several caspases (5,9-12). Inflammatory stimuli, including RNS, increase overall cellular RSNO formation, which further mediates the inflammatory process (9,(13)(14)(15)(16)(17). Direct detection and specific identification of S-nitrosated residues in proteins is essential to better understand RSNO-mediated signaling. Current techniques, such as the biotin switch assay, Saville assay, and chemiluminescencebased methods, are ind...

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Phosphines and Related P–C-bonded Compounds

Allen¹

2010

Organophosphorus Chemistry

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Comparison of the reactivity of N‐(p‐toluenesulfonyl)‐sulfinimidoyl fluorides and chlorides toward triphenylphosphine

Abstract: The path of the reaction of aryl-N-( p-toluenesulfonyl)-sulfinimidoyl fluorides and triphenylphosphine is highly dependent on the order of the reactants addition. Addition of triphenylphosphine

Cited by 3 publications

References 17 publications

Phosphines and related C–P bonded compounds

Phosphines and related C–P bonded compounds

Water-Soluble Triarylphosphines as Biomarkers for Protein S-Nitrosation

Phosphines and Related P–C-bonded Compounds

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