Speciation of reactive sulfur species and their reactions with alkylating agents: do we have any clue about what is present inside the cell?

  Background and Purpose Posttranslational modifications of cysteine residues represent a major aspect of redox biology, and their reliable detection is key in providing mechanistic insights. The metastable character of these modifications and cell lysis‐induced artifactual oxidation render current...

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Published inBritish journal of pharmacology Vol. 176; no. 4; pp. 646 - 670
Main Authors Bogdándi, Virág, Ida, Tomoaki, Sutton, Thomas R, Bianco, Christopher, Ditrói, Tamás, Koster, Grielof, Henthorn, Hillary A, Minnion, Magda, Toscano, John P, Vliet, Albert, Pluth, Michael D, Feelisch, Martin, Fukuto, Jon M, Akaike, Takaaki, Nagy, Péter
Format Journal Article
LanguageEnglish
Published England Blackwell Publishing Ltd 01.02.2019
John Wiley and Sons Inc
Subjects
Adult
Alkylating agents
Alkylating Agents - chemistry
Alkylation
Blood plasma
Cysteine
Glyceraldehyde-3-phosphate dehydrogenase
Humans
Iodoacetamide - chemistry
Labeling
Lysis
Maleimides - chemistry
Methyl Methanesulfonate - analogs & derivatives
Methyl Methanesulfonate - chemistry
Oxidation
Research Paper
Speciation
Species
Sulfenic acid
Sulfides
Sulfur
Sulfur Compounds - analysis
Sulfur Compounds - blood
Sulfur Compounds - chemistry
Themed Section: Research Papers
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Abstract   Background and Purpose Posttranslational modifications of cysteine residues represent a major aspect of redox biology, and their reliable detection is key in providing mechanistic insights. The metastable character of these modifications and cell lysis‐induced artifactual oxidation render current state‐of‐the‐art protocols to rely on alkylation‐based stabilization of labile cysteine derivatives before cell/tissue rupture. An untested assumption in these procedures is that for all cysteine derivatives, alkylation rates are faster than their dynamic interchange. However, when the interconversion of cysteine derivatives is not rate limiting, electrophilic labelling is under Curtin–Hammett control; hence, the final alkylated mixture may not represent the speciation that prevailed before alkylation. Experimental Approach Buffered aqueous solutions of inorganic, organic, cysteine, GSH and GAPDH polysulfide species were used. Additional experiments in human plasma and serum revealed that monobromobimane can extract sulfide from the endogenous sulfur pool by shifting speciation equilibria, suggesting caution should be exercised when interpreting experimental results using this tool. Key Results In the majority of cases, the speciation of alkylated polysulfide/thiol derivatives depended on the experimental conditions. Alkylation perturbed sulfur speciation in both a concentration‐ and time‐dependent manner and strong alkylating agents cleaved polysulfur chains. Moreover, the labelling of sulfenic acids with dimedone also affected cysteine speciation, suggesting that part of the endogenous pool of products previously believed to represent sulfenic acid species may represent polysulfides. Conclusions and Implications We highlight methodological caveats potentially arising from these pitfalls and conclude that current derivatization strategies often fail to adequately capture physiological speciation of sulfur species. Linked Articles This article is part of a themed section on Chemical Biology of Reactive Sulfur Species. To view the other articles in this section visit http://onlinelibrary.wiley.com/doi/10.1111/bph.v176.4/issuetoc
AbstractList Background and PurposePosttranslational modifications of cysteine residues represent a major aspect of redox biology, and their reliable detection is key in providing mechanistic insights. The metastable character of these modifications and cell lysis‐induced artifactual oxidation render current state‐of‐the‐art protocols to rely on alkylation‐based stabilization of labile cysteine derivatives before cell/tissue rupture. An untested assumption in these procedures is that for all cysteine derivatives, alkylation rates are faster than their dynamic interchange. However, when the interconversion of cysteine derivatives is not rate limiting, electrophilic labelling is under Curtin–Hammett control; hence, the final alkylated mixture may not represent the speciation that prevailed before alkylation.Experimental ApproachBuffered aqueous solutions of inorganic, organic, cysteine, GSH and GAPDH polysulfide species were used. Additional experiments in human plasma and serum revealed that monobromobimane can extract sulfide from the endogenous sulfur pool by shifting speciation equilibria, suggesting caution should be exercised when interpreting experimental results using this tool.Key ResultsIn the majority of cases, the speciation of alkylated polysulfide/thiol derivatives depended on the experimental conditions. Alkylation perturbed sulfur speciation in both a concentration‐ and time‐dependent manner and strong alkylating agents cleaved polysulfur chains. Moreover, the labelling of sulfenic acids with dimedone also affected cysteine speciation, suggesting that part of the endogenous pool of products previously believed to represent sulfenic acid species may represent polysulfides.Conclusions and ImplicationsWe highlight methodological caveats potentially arising from these pitfalls and conclude that current derivatization strategies often fail to adequately capture physiological speciation of sulfur species.Linked ArticlesThis article is part of a themed section on Chemical Biology of Reactive Sulfur Species. To view the other articles in this section visit http://onlinelibrary.wiley.com/doi/10.1111/bph.v176.4/issuetoc
  Background and Purpose Posttranslational modifications of cysteine residues represent a major aspect of redox biology, and their reliable detection is key in providing mechanistic insights. The metastable character of these modifications and cell lysis‐induced artifactual oxidation render current state‐of‐the‐art protocols to rely on alkylation‐based stabilization of labile cysteine derivatives before cell/tissue rupture. An untested assumption in these procedures is that for all cysteine derivatives, alkylation rates are faster than their dynamic interchange. However, when the interconversion of cysteine derivatives is not rate limiting, electrophilic labelling is under Curtin–Hammett control; hence, the final alkylated mixture may not represent the speciation that prevailed before alkylation. Experimental Approach Buffered aqueous solutions of inorganic, organic, cysteine, GSH and GAPDH polysulfide species were used. Additional experiments in human plasma and serum revealed that monobromobimane can extract sulfide from the endogenous sulfur pool by shifting speciation equilibria, suggesting caution should be exercised when interpreting experimental results using this tool. Key Results In the majority of cases, the speciation of alkylated polysulfide/thiol derivatives depended on the experimental conditions. Alkylation perturbed sulfur speciation in both a concentration‐ and time‐dependent manner and strong alkylating agents cleaved polysulfur chains. Moreover, the labelling of sulfenic acids with dimedone also affected cysteine speciation, suggesting that part of the endogenous pool of products previously believed to represent sulfenic acid species may represent polysulfides. Conclusions and Implications We highlight methodological caveats potentially arising from these pitfalls and conclude that current derivatization strategies often fail to adequately capture physiological speciation of sulfur species. Linked Articles This article is part of a themed section on Chemical Biology of Reactive Sulfur Species. To view the other articles in this section visit http://onlinelibrary.wiley.com/doi/10.1111/bph.v176.4/issuetoc
  Background and Purpose Posttranslational modifications of cysteine residues represent a major aspect of redox biology, and their reliable detection is key in providing mechanistic insights. The metastable character of these modifications and cell lysis‐induced artifactual oxidation render current state‐of‐the‐art protocols to rely on alkylation‐based stabilization of labile cysteine derivatives before cell/tissue rupture. An untested assumption in these procedures is that for all cysteine derivatives, alkylation rates are faster than their dynamic interchange. However, when the interconversion of cysteine derivatives is not rate limiting, electrophilic labelling is under Curtin–Hammett control; hence, the final alkylated mixture may not represent the speciation that prevailed before alkylation. Experimental Approach Buffered aqueous solutions of inorganic, organic, cysteine, GSH and GAPDH polysulfide species were used. Additional experiments in human plasma and serum revealed that monobromobimane can extract sulfide from the endogenous sulfur pool by shifting speciation equilibria, suggesting caution should be exercised when interpreting experimental results using this tool. Key Results In the majority of cases, the speciation of alkylated polysulfide/thiol derivatives depended on the experimental conditions. Alkylation perturbed sulfur speciation in both a concentration‐ and time‐dependent manner and strong alkylating agents cleaved polysulfur chains. Moreover, the labelling of sulfenic acids with dimedone also affected cysteine speciation, suggesting that part of the endogenous pool of products previously believed to represent sulfenic acid species may represent polysulfides. Conclusions and Implications We highlight methodological caveats potentially arising from these pitfalls and conclude that current derivatization strategies often fail to adequately capture physiological speciation of sulfur species. Linked Articles This article is part of a themed section on Chemical Biology of Reactive Sulfur Species. To view the other articles in this section visit http://onlinelibrary.wiley.com/doi/10.1111/bph.v176.4/issuetoc
BACKGROUND AND PURPOSE: Posttranslational modifications of cysteine residues represent a major aspect of redox biology, and their reliable detection is key in providing mechanistic insights. The metastable character of these modifications and cell lysis-induced artifactual oxidation render current state-of-the-art protocols to rely on alkylation-based stabilization of labile cysteine derivatives before cell/tissue rupture. An untested assumption in these procedures is that for all cysteine derivatives, alkylation rates are faster than their dynamic interchange. However, when the interconversion of cysteine derivatives is not rate limiting, electrophilic labelling is under Curtin-Hammett control; hence, the final alkylated mixture may not represent the speciation that prevailed before alkylation. Buffered aqueous solutions of inorganic, organic, cysteine, GSH and GAPDH polysulfide species were used. Additional experiments in human plasma and serum revealed that monobromobimane can extract sulfide from the endogenous sulfur pool by shifting speciation equilibria, suggesting caution should be exercised when interpreting experimental results using this tool. In the majority of cases, the speciation of alkylated polysulfide/thiol derivatives depended on the experimental conditions. Alkylation perturbed sulfur speciation in both a concentration- and time-dependent manner and strong alkylating agents cleaved polysulfur chains. Moreover, the labelling of sulfenic acids with dimedone also affected cysteine speciation, suggesting that part of the endogenous pool of products previously believed to represent sulfenic acid species may represent polysulfides. We highlight methodological caveats potentially arising from these pitfalls and conclude that current derivatization strategies often fail to adequately capture physiological speciation of sulfur species. This article is part of a themed section on Chemical Biology of Reactive Sulfur Species. To view the other articles in this section visit http://onlinelibrary.wiley.com/doi/10.1111/bph.v176.4/issuetoc.
Author Minnion, Magda
Bianco, Christopher
Vliet, Albert
Sutton, Thomas R
Pluth, Michael D
Koster, Grielof
Fukuto, Jon M
Ida, Tomoaki
Bogdándi, Virág
Ditrói, Tamás
Toscano, John P
Feelisch, Martin
Henthorn, Hillary A
Nagy, Péter
Akaike, Takaaki
AuthorAffiliation 4 Department of Chemistry Johns Hopkins University Baltimore MD USA
7 Department of Chemistry Sonoma State University Rohnert Park CA USA
6 Department of Pathology and Laboratory Medicine, Robert Larner, M.D. College of Medicine University of Vermont Burlington VT USA
1 Department of Molecular Immunology and Toxicology National Institute of Oncology Budapest Hungary
2 Department of Environmental Medicine and Molecular Toxicology Tohoku University Graduate School of Medicine Sendai Japan
3 Clinical and Experimental Sciences, Faculty of Medicine University Hospital Southampton NHS Foundation Trust, University of Southampton Southampton UK
5 Department of Chemistry and Biochemistry, Materials Science Institute, Institute of Molecular Biology University of Oregon Eugene OR USA
AuthorAffiliation_xml – name: 4 Department of Chemistry Johns Hopkins University Baltimore MD USA
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– name: 6 Department of Pathology and Laboratory Medicine, Robert Larner, M.D. College of Medicine University of Vermont Burlington VT USA
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  organization: University of Oregon
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  surname: Minnion
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  organization: University Hospital Southampton NHS Foundation Trust, University of Southampton
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  organization: Johns Hopkins University
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  orcidid: 0000-0003-3604-653X
  surname: Pluth
  fullname: Pluth, Michael D
  organization: University of Oregon
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  surname: Feelisch
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  organization: National Institute of Oncology
BackLink https://www.ncbi.nlm.nih.gov/pubmed/29909607$$D View this record in MEDLINE/PubMed
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Cites_doi 10.1021/ja0737218
10.1126/sciadv.1500968
10.1126/science.233.4763.563
10.1016/j.bbrc.2016.10.022
10.1016/0013-4686(59)80009-8
10.1021/es062637
10.1038/nchembio.1834
10.1016/0016-7037(63)90050-4
10.1111/bph.12769
10.1021/tx100266a
10.1016/j.ab.2011.01.044
10.1111/bph.14372
10.1007/s00604-004-0179-5
10.1111/bph.12369
10.1051/water/19780901027
10.1016/j.redox.2018.02.012
10.1016/bs.mie.2014.11.036
10.1126/scisignal.290re7
10.1089/ars.2010.3678
10.1093/oxfordjournals.jbchem.a133393
10.1038/s41467-017-01311-y
10.1021/ed063p42
10.1016/j.bbagen.2013.05.037
10.1021/jacs.6b03456
10.1111/bph.14153
10.1021/bi300778t
10.1002/anie.201305876
10.1073/pnas.1509277112
10.1021/ac051854a
10.1074/jbc.M115.672816
10.1007/b13183
10.1021/ic50116a047
10.1016/0165-022X(86)90102-8
10.1021/ic00235a003
10.1126/scisignal.2000464
10.1073/pnas.1321232111
10.1089/ars.2017.7076
10.1016/j.freeradbiomed.2017.10.384
10.1016/j.redox.2017.10.006
10.1016/j.freeradbiomed.2013.01.021
10.1016/j.freeradbiomed.2014.09.007
10.1021/cr300163e
10.1016/j.abb.2011.09.015
10.1074/jbc.M117.774943
10.1007/b13182
10.1021/acs.inorgchem.6b01660
10.3891/acta.chem.scand.53-0513
10.1016/S1872-0854(10)04006-3
10.1021/es049514e
10.1093/nar/gkx1121
10.1039/C5DT03355A
10.1111/j.1751-908X.2009.00907.x
10.1039/c3cs60119f
10.1016/j.redox.2017.10.012
10.1016/B978-1-4831-9982-5.50004-X
10.1021/ic50112a009
10.1016/B978-0-12-804273-1.00005-3
10.1038/330148a0
10.1016/j.freeradbiomed.2010.10.705
10.1038/srep29808
10.1038/srep45995
10.1038/nrm3391
10.1146/annurev.pharmtox.44.101802.121735
10.1016/j.freeradbiomed.2013.02.017
10.7554/eLife.10067
10.1016/j.freeradbiomed.2011.01.025
10.1111/bph.12368
10.1111/bph.13877
10.1089/ars.2012.5041
10.1089/ars.2017.7083
10.1016/j.redox.2017.02.021
10.1016/j.freeradbiomed.2015.08.017
10.1038/ncomms13386
10.1111/j.1476-5381.2010.00704.x
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2018 The British Pharmacological Society.
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2015; 4
2003b; 231
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1986; 233
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References_xml – volume: 14
  start-page: 485
  year: 2018
  end-page: 491
  article-title: Chemical trapping and characterization of small oxoacids of sulfur (SOS) generated in aqueous oxidations of H S
  publication-title: Redox Biol
– volume: 554
  start-page: 3
  year: 2015
  end-page: 29
  article-title: Mechanistic chemical perspective of hydrogen sulfide signaling
  publication-title: Methods Enzymol
– volume: 60
  start-page: 325
  year: 2013
  end-page: 335
  article-title: Exposing cells to H O : a quantitative comparison between continuous low‐dose and one‐time high‐dose treatments
  publication-title: Free Radic Biol Med
– volume: 51
  start-page: 6804
  year: 2012
  end-page: 6815
  article-title: Human sulfide: quinone oxidoreductase catalyzes the first step in hydrogen sulfide metabolism and produces a sulfane sulfur metabolite
  publication-title: Biochemistry
– volume: 27
  start-page: 684
  year: 2017
  end-page: 712
  article-title: The reactive species interactome: evolutionary emergence, biological significance, and opportunities for redox metabolomics and personalized medicine
  publication-title: Antioxid Redox Signal
– volume: 292
  start-page: 5584
  year: 2017
  end-page: 5592
  article-title: Structural and mechanistic insights into hemoglobin‐catalyzed hydrogen sulfide oxidation and the fate of polysulfide products
  publication-title: J Biol Chem
– volume: 160
  start-page: 941
  year: 2010
  end-page: 957
  article-title: A monobromobimane‐based assay to measure the pharmacokinetic profile of reactive sulphide species in blood
  publication-title: Br J Pharmacol
– volume: 7
  year: 2017
  article-title: Polysulfides (H Sn) produced from the interaction of hydrogen sulfide (H S) and nitric oxide (NO) activate TRPA1 channels
  publication-title: Sci Rep
– volume: 19
  start-page: 1749
  year: 2013
  end-page: 1765
  article-title: Polysulfides link H S to protein thiol oxidation
  publication-title: Antioxid Redox Signal
– volume: 12
  start-page: 325
  year: 2017
  end-page: 339
  article-title: Catalase as a sulfide‐sulfur oxido‐reductase: an ancient (and modern?) regulator of reactive sulfur species (RSS)
  publication-title: Redox Biol
– volume: 44
  start-page: 19782
  year: 2015
  end-page: 19785
  article-title: NBu SH provides a convenient source of HS soluble in organic solution for H S and anion‐binding research
  publication-title: Dalton Trans
– volume: 6
  year: 2016
  article-title: Quantitative persulfide site identification (qPerS‐SID) reveals protein targets of H S releasing donors in mammalian cells
  publication-title: Sci Rep
– volume: 63
  start-page: 42
  year: 1986
  article-title: The Curtin–Hammett principle and the Winstein–Holness equation: new definition and recent extensions to classical concepts
  publication-title: J Chem Educ
– volume: 112
  start-page: E4651
  year: 2015
  end-page: E4660
  article-title: Key bioactive reaction products of the NO/H S interaction are S/N‐hybrid species, polysulfides, and nitroxyl
  publication-title: P Natl Acad Sci USA
– volume: 14
  start-page: 379
  year: 2017
  end-page: 385
  article-title: Cysteine perthiosulfenic acid (Cys‐SSOH): a novel intermediate in thiol‐based redox signaling?
  publication-title: Redox Biol
– volume: 516
  start-page: 146
  year: 2011
  end-page: 153
  article-title: The reaction of H S with oxidized thiols: generation of persulfides and implications to H S biology
  publication-title: Arch Biochem Biophys
– volume: 171
  start-page: 2099
  year: 2014
  end-page: 2122
  article-title: Regulation of mitochondrial bioenergetic function by hydrogen sulfide. Part I. Biochemical and physiological mechanisms
  publication-title: Br J Pharmacol
– volume: 111
  start-page: 7606
  year: 2014
  end-page: 7611
  article-title: Reactive cysteine persulfides and ‐polythiolation regulate oxidative stress and redox signaling
  publication-title: P Natl Acad Sci USA
– volume: 330
  start-page: 148
  year: 1987
  end-page: 151
  article-title: A description of energy conversion in photoelectrochemical solar cells
  publication-title: Nature
– volume: 42
  start-page: 5996
  year: 2013
  end-page: 6005
  article-title: Ubiquitous trisulfur radical anion: fundamentals and applications in materials science, electrochemistry, analytical chemistry and geochemistry
  publication-title: Chem Soc Rev
– volume: 4
  year: 2015
  article-title: Quantitative H S‐mediated protein sulfhydration reveals metabolic reprogramming during the integrated stress response
  publication-title: Elife
– start-page: 57
  year: 2017
  end-page: 83
– volume: 2
  start-page: ra72
  year: 2009
  article-title: H S signals through protein ‐sulfhydration
  publication-title: Sci Signal
– volume: 231
  start-page: 99
  year: 2003b
  end-page: 125
  article-title: Inorganic polysulfanes H2Sn with n > 1
  publication-title: Top Curr Chem
– volume: 176
  start-page: 671
  year: 2019
  end-page: 683
  article-title: The reaction of hydrogen sulfide with disulfides: formation of a stable trisulfide and implications to biological systems
  publication-title: Br J Pharmacol
– volume: 11
  start-page: 457
  year: 2015
  end-page: 464
  article-title: Biogenesis of reactive sulfur species for signaling by hydrogen sulfide oxidation pathways
  publication-title: Nat Chem Biol
– volume: 2
  year: 2016
  article-title: A novel persulfide detection method reveals protein persulfide‐ and polysulfide‐reducing functions of thioredoxin and glutathione systems
  publication-title: Sci Adv
– volume: 172
  start-page: 1516
  year: 2015
  end-page: 1532
  article-title: Interactions of hydrogen sulfide with myeloperoxidase
  publication-title: Br J Pharmacol
– volume: 231
  start-page: 127
  year: 2003a
  end-page: 152
  article-title: Inorganic polysulfides S‐n(2‐) and radical anions S‐n (center dot‐)
  publication-title: Top Curr Chem
– volume: 78
  start-page: 2631
  year: 2006
  end-page: 2639
  article-title: Method for the determination of inorganic polysulfide distribution in aquatic systems
  publication-title: Anal Chem
– volume: 20
  start-page: 113
  year: 1822
  end-page: 141
  article-title: De la Composition des Sulfures Alcalins
  publication-title: Ann Chim Phys
– volume: 175
  start-page: 987
  year: 2018
  end-page: 993
  article-title: Experimental design and analysis and their reporting II: updated and simplified guidance for authors and peer reviewers
  publication-title: Br J Pharmacol
– volume: 46
  start-page: D1091
  year: 2018
  end-page: D1106
  article-title: The IUPHAR/BPS Guide to PHARMACOLOGY in 2018: updates and expansion to encompass the new guide to IMMUNOPHARMACOLOGY
  publication-title: Nucleic Acids Res
– volume: 53
  start-page: 513
  year: 1999
  end-page: 520
  article-title: Nucleophilic substitution of alkyl halides by electrogenerated polysulfide ions in , ‐dimethylacetamide
  publication-title: Acta Chem Scand
– volume: 23
  start-page: 1541
  year: 2010a
  end-page: 1543
  article-title: Rapid reaction of hydrogen sulfide with the neutrophil oxidant hypochlorous acid to generate polysulfides
  publication-title: Chem Res Toxicol
– volume: 171
  start-page: 2123
  year: 2014
  end-page: 2146
  article-title: Regulation of mitochondrial bioenergetic function by hydrogen sulfide. Part II. Pathophysiological and therapeutic aspects
  publication-title: Br J Pharmacol
– volume: 174
  start-page: S272
  year: 2017
  end-page: S359
  article-title: The Concise Guide To PHARMACOLOGY 2017/18: Enzymes
  publication-title: Br J Pharmacol
– volume: 89
  start-page: 1913
  year: 1981
  end-page: 1921
  article-title: The mechanism of the ‐cystine cleavage reaction catalyzed by rat liver γ‐cystathionase
  publication-title: J Biochem
– volume: 15
  start-page: 379
  year: 2011
  end-page: 391
  article-title: Mitochondria and sulfide: a very old story of poisoning, feeding, and signaling?
  publication-title: Antioxid Redox Signal
– volume: 50
  start-page: 1021
  year: 2011
  end-page: 1031
  article-title: Measurement of plasma hydrogen sulfide in vivo and in vitro
  publication-title: Free Radic Biol Med
– volume: 55
  start-page: 12618
  year: 2016
  end-page: 12625
  article-title: The intersection of NO and H S: persulfides generate NO from nitrite through polysulfide formation
  publication-title: Inorg Chem
– volume: 16
  start-page: 359
  year: 2018
  end-page: 380
  article-title: A robust and versatile mass spectrometry platform for comprehensive assessment of the thiol redox metabolome
  publication-title: Redox Biol
– volume: 480
  start-page: 180
  year: 2016
  end-page: 186
  article-title: Protein polysulfidation‐dependent persulfide dioxygenase activity of ethylmalonic encephalopathy protein 1
  publication-title: Biochem Biophys Res Commun
– volume: 138
  start-page: 8476
  year: 2016
  end-page: 8488
  article-title: Hydrogen sulfide oxidation by myoglobin
  publication-title: J Am Chem Soc
– volume: 58
  start-page: 109
  year: 2013
  end-page: 117
  article-title: Redox proteomics of thiol proteins in mouse heart during ischemia/reperfusion using ICAT reagents and mass spectrometry
  publication-title: Free Radic Biol Med
– volume: 2
  start-page: re7
  year: 2009
  article-title: Transduction of redox signaling by electrophile–protein reactions
  publication-title: Sci Signal
– volume: 33
  start-page: 415
  year: 2009
  end-page: 435
  article-title: Protocol for quantitative detection of elemental sulfur and polysulfide zero‐valent sulfur distribution in natural aquatic samples
  publication-title: Geostand Geoanal Res
– volume: 46
  start-page: 93
  year: 2015
  end-page: 101
  article-title: Kinetic and thermodynamic studies on the disulfide‐bond reducing potential of hydrogen sulfide. Nitric oxide: biology and chemistry/official journal of the Nitric Oxide
  publication-title: Society
– volume: 1840
  start-page: 876
  year: 2014
  end-page: 891
  article-title: Chemical aspects of hydrogen sulfide measurements in physiological samples
  publication-title: Biochim Biophys Acta
– volume: 53
  start-page: 575
  year: 2014
  end-page: 581
  article-title: Detection of protein ‐sulfhydration by a tag‐switch technique
  publication-title: Angew Chem Int Ed Engl
– volume: 27
  start-page: 1265
  year: 1963
  end-page: 1298
  article-title: The geologic role of polysulfides – part I. The distribution of ionic species in aqueous sodium polysulfide solutions
  publication-title: Geochim Cosmochim Acta
– volume: 77
  start-page: 82
  year: 2014
  end-page: 94
  article-title: Redox chemistry and chemical biology of H S, hydropersulfides, and derived species: implications of their possible biological activity and utility
  publication-title: Free Radic Biol Med
– volume: 44
  start-page: 325
  year: 2004
  end-page: 347
  article-title: Protein sulfenic acids in redox signaling
  publication-title: Annu Rev Pharmacol Toxicol
– volume: 50
  start-page: 196
  year: 2011
  end-page: 205
  article-title: Reactivity of hydrogen sulfide with peroxynitrite and other oxidants of biological interest
  publication-title: Free Radic Biol Med
– volume: 7
  year: 2016
  article-title: Sulfheme formation during homocysteine S‐oxygenation by catalase in cancers and neurodegenerative diseases
  publication-title: Nat Commun
– volume: 27
  start-page: 619
  year: 2017
  end-page: 621
  article-title: Hydrogen sulfide and polysulfide signaling
  publication-title: Antioxid Redox Signal
– volume: 11
  start-page: 2525
  year: 1972
  end-page: 2527
  article-title: Characterization of the trisulfur radical anion S3− in blue solutions of alkali polysulfides in hexamethylphosphoramide
  publication-title: Inorg Chem
– volume: 233
  start-page: 563
  year: 1986
  end-page: 566
  article-title: Hydrogen sulfide oxidation is coupled to oxidative phosphorylation in mitochondria of
  publication-title: Science
– volume: 113
  start-page: 4633
  year: 2013
  end-page: 4679
  article-title: Cysteine‐mediated redox signaling: chemistry, biology, and tools for discovery
  publication-title: Chem Rev
– volume: 129
  start-page: 14082
  year: 2007
  end-page: 14091
  article-title: Reactive sulfur species: kinetics and mechanisms of the oxidation of cysteine by hypohalous acid to give cysteine sulfenic acid
  publication-title: J Am Chem Soc
– volume: 4
  start-page: 183
  year: 2010b
  end-page: 222
  article-title: Redox chemistry of biological thiols
  publication-title: Advances in Molecular Toxicology
– start-page: 1
  year: 1961
  end-page: 6
– volume: 25
  start-page: 2486
  year: 1986
  end-page: 2489
  article-title: Numerical analysis of aqueous polysulfide solutions and its application to cadmium chalcogenide polysulfide photoelectrochemical solar cells
  publication-title: Inorg Chem
– volume: 146
  start-page: 229
  year: 2004
  end-page: 237
  article-title: Electrospray ionization mass spectrometric analysis of aqueous polysulfide solutions
  publication-title: Microchim Acta
– volume: 113
  start-page: 551
  year: 2017
  end-page: 563
  article-title: Mechanisms of myeloperoxidase catalyzed oxidation of H S by H O or O to produce potent protein Cys‐polysulfide‐inducing species
  publication-title: Free Radic Biol Med
– volume: 1
  start-page: 58
  year: 1959
  end-page: 69
  article-title: Constantes de dissociation de l'hydrogène sulfuré
  publication-title: Electrochim Acta
– volume: 89
  start-page: 662
  year: 2015
  end-page: 667
  article-title: Reactions of isolated persulfides provide insights into the interplay between H S and persulfide reactivity
  publication-title: Free Radic Biol Med
– volume: 9
  start-page: 24
  year: 1978
  end-page: 33
  article-title: Constantes de formation des ions polysulfures S‐26, S‐25 et S‐24 en phase aqueuse
  publication-title: J Fr Hydrol
– year: 2017
– volume: 41
  start-page: 2395
  year: 2007
  end-page: 2400
  article-title: Equilibrium distribution of polysulfide ions in aqueous solutions at different temperatures by rapid single phase derivatization
  publication-title: Environ Sci Technol
– volume: 413
  start-page: 1
  year: 2011
  end-page: 7
  article-title: Sulfur signaling: is the agent sulfide or sulfane?
  publication-title: Anal Biochem
– volume: 13
  start-page: 499
  year: 2012
  end-page: 507
  article-title: H S signalling through protein sulfhydration and beyond
  publication-title: Nat Rev Mol Cell Biol
– volume: 11
  start-page: 1201
  year: 1972
  end-page: 1207
  article-title: Optical spectra and equilibrium distribution of polysulfide ions in aqueous solution at 20.deg
  publication-title: Inorg Chem
– year: 1777
– volume: 13
  start-page: 231
  year: 1986
  end-page: 249
  article-title: Methodologies for the application of monobromobimane to the simultaneous analysis of soluble and protein thiol components of biological systems
  publication-title: J Biochem Biophys Methods
– volume: 290
  start-page: 26866
  year: 2015
  end-page: 26880
  article-title: Reaction of hydrogen sulfide with disulfide and sulfenic acid to form the strongly nucleophilic persulfide
  publication-title: J Biol Chem
– volume: 8
  start-page: 1177
  year: 2017
  article-title: Cysteinyl‐tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics
  publication-title: Nat Commun
– volume: 38
  start-page: 6633
  year: 2004
  end-page: 6644
  article-title: Equilibrium distribution of polysulfide ions in aqueous solutions at 25 degrees C: a new approach for the study of polysulfides' equilibria
  publication-title: Environ Sci Technol
– ident: e_1_2_9_53_1
  doi: 10.1021/ja0737218
– volume-title: Methods in Molecular Biology
  year: 2017
  ident: e_1_2_9_21_1
  contributor:
    fullname: Doka E
– ident: e_1_2_9_22_1
  doi: 10.1126/sciadv.1500968
– ident: e_1_2_9_64_1
  doi: 10.1126/science.233.4763.563
– ident: e_1_2_9_35_1
  doi: 10.1016/j.bbrc.2016.10.022
– ident: e_1_2_9_47_1
  doi: 10.1016/0013-4686(59)80009-8
– ident: e_1_2_9_39_1
  doi: 10.1021/es062637
– ident: e_1_2_9_48_1
  doi: 10.1038/nchembio.1834
– ident: e_1_2_9_15_1
  doi: 10.1016/0016-7037(63)90050-4
– ident: e_1_2_9_60_1
  doi: 10.1111/bph.12769
– ident: e_1_2_9_54_1
  doi: 10.1021/tx100266a
– ident: e_1_2_9_74_1
  doi: 10.1016/j.ab.2011.01.044
– ident: e_1_2_9_8_1
  doi: 10.1111/bph.14372
– ident: e_1_2_9_29_1
  doi: 10.1007/s00604-004-0179-5
– ident: e_1_2_9_73_1
  doi: 10.1111/bph.12369
– ident: e_1_2_9_11_1
  doi: 10.1051/water/19780901027
– ident: e_1_2_9_66_1
– ident: e_1_2_9_72_1
  doi: 10.1016/j.redox.2018.02.012
– ident: e_1_2_9_52_1
  doi: 10.1016/bs.mie.2014.11.036
– ident: e_1_2_9_65_1
  doi: 10.1126/scisignal.290re7
– ident: e_1_2_9_10_1
  doi: 10.1089/ars.2010.3678
– ident: e_1_2_9_78_1
  doi: 10.1093/oxfordjournals.jbchem.a133393
– ident: e_1_2_9_3_1
  doi: 10.1038/s41467-017-01311-y
– ident: e_1_2_9_67_1
  doi: 10.1021/ed063p42
– ident: e_1_2_9_56_1
  doi: 10.1016/j.bbagen.2013.05.037
– ident: e_1_2_9_9_1
  doi: 10.1021/jacs.6b03456
– ident: e_1_2_9_20_1
  doi: 10.1111/bph.14153
– ident: e_1_2_9_34_1
  doi: 10.1021/bi300778t
– ident: e_1_2_9_79_1
  doi: 10.1002/anie.201305876
– ident: e_1_2_9_17_1
  doi: 10.1073/pnas.1509277112
– ident: e_1_2_9_37_1
  doi: 10.1021/ac051854a
– ident: e_1_2_9_19_1
  doi: 10.1074/jbc.M115.672816
– ident: e_1_2_9_70_1
  doi: 10.1007/b13183
– ident: e_1_2_9_13_1
  doi: 10.1021/ic50116a047
– ident: e_1_2_9_18_1
  doi: 10.1016/0165-022X(86)90102-8
– ident: e_1_2_9_45_1
  doi: 10.1021/ic00235a003
– ident: e_1_2_9_51_1
  doi: 10.1126/scisignal.2000464
– ident: e_1_2_9_33_1
  doi: 10.1073/pnas.1321232111
– ident: e_1_2_9_41_1
  doi: 10.1089/ars.2017.7076
– ident: e_1_2_9_26_1
  doi: 10.1016/j.freeradbiomed.2017.10.384
– ident: e_1_2_9_32_1
  doi: 10.1016/j.redox.2017.10.006
– ident: e_1_2_9_43_1
  doi: 10.1016/j.freeradbiomed.2013.01.021
– ident: e_1_2_9_58_1
  doi: 10.1016/j.freeradbiomed.2014.09.007
– ident: e_1_2_9_62_1
  doi: 10.1021/cr300163e
– ident: e_1_2_9_24_1
  doi: 10.1016/j.abb.2011.09.015
– ident: e_1_2_9_76_1
  doi: 10.1074/jbc.M117.774943
– ident: e_1_2_9_71_1
  doi: 10.1007/b13182
– ident: e_1_2_9_6_1
  doi: 10.1021/acs.inorgchem.6b01660
– ident: e_1_2_9_2_1
  doi: 10.3891/acta.chem.scand.53-0513
– ident: e_1_2_9_55_1
  doi: 10.1016/S1872-0854(10)04006-3
– ident: e_1_2_9_38_1
  doi: 10.1021/es049514e
– volume: 20
  start-page: 113
  year: 1822
  ident: e_1_2_9_7_1
  article-title: De la Composition des Sulfures Alcalins
  publication-title: Ann Chim Phys
  contributor:
    fullname: Berzelius J
– ident: e_1_2_9_30_1
  doi: 10.1093/nar/gkx1121
– ident: e_1_2_9_31_1
  doi: 10.1039/C5DT03355A
– ident: e_1_2_9_36_1
  doi: 10.1111/j.1751-908X.2009.00907.x
– ident: e_1_2_9_14_1
  doi: 10.1039/c3cs60119f
– ident: e_1_2_9_42_1
  doi: 10.1016/j.redox.2017.10.012
– ident: e_1_2_9_23_1
  doi: 10.1016/B978-1-4831-9982-5.50004-X
– ident: e_1_2_9_27_1
  doi: 10.1021/ic50112a009
– ident: e_1_2_9_40_1
  doi: 10.1016/B978-0-12-804273-1.00005-3
– ident: e_1_2_9_44_1
  doi: 10.1038/330148a0
– ident: e_1_2_9_12_1
  doi: 10.1016/j.freeradbiomed.2010.10.705
– ident: e_1_2_9_46_1
  doi: 10.1038/srep29808
– ident: e_1_2_9_49_1
  doi: 10.1038/srep45995
– ident: e_1_2_9_61_1
  doi: 10.1038/nrm3391
– ident: e_1_2_9_63_1
  doi: 10.1146/annurev.pharmtox.44.101802.121735
– ident: e_1_2_9_69_1
  doi: 10.1016/j.freeradbiomed.2013.02.017
– ident: e_1_2_9_25_1
  doi: 10.7554/eLife.10067
– ident: e_1_2_9_68_1
  doi: 10.1016/j.freeradbiomed.2011.01.025
– ident: e_1_2_9_50_1
  doi: 10.1111/bph.12368
– ident: e_1_2_9_4_1
  doi: 10.1111/bph.13877
– ident: e_1_2_9_28_1
  doi: 10.1089/ars.2012.5041
– ident: e_1_2_9_16_1
  doi: 10.1089/ars.2017.7083
– ident: e_1_2_9_57_1
  doi: 10.1016/j.redox.2017.02.021
– ident: e_1_2_9_5_1
  doi: 10.1016/j.freeradbiomed.2015.08.017
– volume: 46
  start-page: 93
  year: 2015
  ident: e_1_2_9_75_1
  article-title: Kinetic and thermodynamic studies on the disulfide‐bond reducing potential of hydrogen sulfide. Nitric oxide: biology and chemistry/official journal of the Nitric Oxide
  publication-title: Society
  contributor:
    fullname: Vasas A
– ident: e_1_2_9_59_1
  doi: 10.1038/ncomms13386
– ident: e_1_2_9_77_1
  doi: 10.1111/j.1476-5381.2010.00704.x
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Snippet   Background and Purpose Posttranslational modifications of cysteine residues represent a major aspect of redox biology, and their reliable detection is key in...
BACKGROUND AND PURPOSE: Posttranslational modifications of cysteine residues represent a major aspect of redox biology, and their reliable detection is key in...
Background and PurposePosttranslational modifications of cysteine residues represent a major aspect of redox biology, and their reliable detection is key in...
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StartPage 646
SubjectTerms Adult
Alkylating agents
Alkylating Agents - chemistry
Alkylation
Blood plasma
Cysteine
Glyceraldehyde-3-phosphate dehydrogenase
Humans
Iodoacetamide - chemistry
Labeling
Lysis
Maleimides - chemistry
Methyl Methanesulfonate - analogs & derivatives
Methyl Methanesulfonate - chemistry
Oxidation
Research Paper
Speciation
Species
Sulfenic acid
Sulfides
Sulfur
Sulfur Compounds - analysis
Sulfur Compounds - blood
Sulfur Compounds - chemistry
Themed Section: Research Papers
Title Speciation of reactive sulfur species and their reactions with alkylating agents: do we have any clue about what is present inside the cell?
URI https://onlinelibrary.wiley.com/doi/abs/10.1111%2Fbph.14394
https://www.ncbi.nlm.nih.gov/pubmed/29909607
https://www.proquest.com/docview/2296308818
https://pubmed.ncbi.nlm.nih.gov/PMC6346080
Volume 176
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