Fast Reductive Ligation of <i>S</i>‐Nitrosothiols

Wang, Hua; Xian, Ming

doi:10.1002/anie.200801654

Cited by 74 publications

(72 citation statements)

References 44 publications

(14 reference statements)

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“…Organophosphine compounds equipped with electrophilic traps were found to mediate chemical ligations of S -nitrosothiols and have been exploited as a detection tool for small molecule and protein SNOs [188–191] and for the quantification of intracellular GSNO [192]. In addition, the use of fully aqueous soluble, sterically hindered organophosphine tris (4,6-dimethyl-3-sulfonatophenyl)phosphine trisodium salt hydrate (TXPTS), that does not possess an electrophilic trap, was also demonstrated to react with S -nitrosothiols, yielding a unique covalent adduct [42].…”

Section: Analysis Of Thiol Chemistry In Complex Systems Using Msmentioning

confidence: 99%

Mass spectrometry in studies of protein thiol chemistry and signaling: Opportunities and caveats

Baez

Reisz

Furdui

2015

Free Radical Biology and Medicine

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Mass spectrometry (MS) has become a powerful and widely utilized tool in the investigation of protein thiol chemistry, biochemistry, and biology. Very early biochemical studies of metabolic enzymes have brought to light the broad spectrum of reactivity profiles that distinguish cysteine thiols with functions in catalysis and protein stability from other cysteine residues in proteins. The development of MS methods for the analysis of proteins using electrospray ionization (ESI) or matrix-assisted laser desorption/ionization (MALDI) coupled with the emergence of high-resolution mass analyzers have been instrumental in advancing studies of thiol modifications, both in single proteins and within the cellular context. This article reviews MS instrumentation and methods of analysis employed in investigations of thiols and their reactivity toward a range of small biomolecules. A selected number of studies are detailed to highlight the advantages brought about by the MS technologies along with the caveats associated with these analyses.

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Section: Analysis Of Thiol Chemistry In Complex Systems Using Msmentioning

confidence: 99%

Mass spectrometry in studies of protein thiol chemistry and signaling: Opportunities and caveats

Baez

Reisz

Furdui

2015

Free Radical Biology and Medicine

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“…These include the SNO-RAC and d-Switch methodologies, which introduce resin-assisted capture and isotopic labeling, to identify and quantify S -nitrosated species from proteomes (Fares et al, 2014; Forrester et al, 2009b; Sinha et al, 2010). Furthermore, protein S -nitrosothiols can be enriched with mercury resin (Doulias et al, 2013; Gould et al, 2015), phosphine reagents that undergo a Staudinger-type reaction (Bechtold et al, 2010; Seneviratne et al, 2013; Seneviratne et al, 2016; Wang and Xian, 2008), and biotinylated sulfinic acids that form stable thiosulfonates (Majmudar et al, 2016). …”

Section: Introductionmentioning

confidence: 99%

Chemoproteomic Strategy to Quantitatively Monitor Transnitrosation Uncovers Functionally Relevant S -Nitrosation Sites on Cathepsin D and HADH2

Zhou

Wynia-Smith

Couvertier

et al. 2016

Cell Chemical Biology

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Summary S-nitrosoglutathione (GSNO) is an endogenous transnitrosation donor involved in S-nitrosation of a variety of cellular proteins, thereby regulating diverse protein functions. Quantitative proteomic methods are necessary to establish which cysteine residues are most sensitive to GSNO-mediated transnitrosation. Here, a competitive cysteine-reactivity profiling strategy was implemented to quantitatively measure the sensitivity of >600 cysteine residues to transnitrosation by GSNO. This platform identified a subset of cysteine residues with a high propensity for GSNO-mediated transnitrosation. Functional characterization of previously unannotated S-nitrosation sites revealed that S-nitrosation of a cysteine residue distal to the 3-hydroxyacyl-CoA dehydrogenase type-2 (HADH2) active site impaired catalytic activity. Similarly, S-nitrosation of a non-catalytic cysteine residue in the lysosomal aspartyl protease cathepsin D (CTSD) inhibited proteolytic activation. Together, these studies revealed two previously uncharacterized cysteine residues that regulate protein function and established a chemical-proteomic platform with capabilities to determine substrate specificity of other cellular transnitrosation agents.

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“…In the past several years our laboratory has developed a series of phosphine-based bioorthogonal reactions of SNO. 4 These reactions specifically target SNO groups and can directly convert unstable SNO to stable and detectable species. While we are continuing to work on these reactions (our goal is to utilize these reactions to develop novel reagents for direct enriching or labeling protein SNO), we realized that fluorescent probes may be developed based on these reactions.…”

mentioning

confidence: 99%

“…4a SNO can react with triaryl phosphine 1 to form the azaylide intermediate 2 , which in turn undergoes a rapid intramolecular acyl transfer and hydrolysis to furnish a sulfenamide 3 and R′OH. This reaction provides a unique and specific way to remove the acylated group on hydroxyl groups.…”

mentioning

confidence: 99%