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Cas Database

70-18-8

70-18-8

Identification

  • Product Name:Glutathione

  • CAS Number: 70-18-8

  • EINECS:200-725-4

  • Molecular Weight:307.327

  • Molecular Formula: C10H17N3O6S

  • HS Code:29309070

  • Mol File:70-18-8.mol

Synonyms:Glutathione(8CI);Glycine, N-(N-L-g-glutamyl-L-cysteinyl)-;Copren;Glutathion;Glutathione-SH;Glutide;Glutinal;Isethion;L-Glutathione;N-(N-L-g-Glutamyl-L-cysteinyl)glycine;Tathione;g-Glutamylcysteinylglycine;g-L-Glutamyl-L-cysteinylglycine;Glycine, L-g-glutamyl-L-cysteinyl-;GSH;L-Glutathione Reduced;

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Safety information and MSDS view more

  • Pictogram(s):IrritantXi

  • Hazard Codes:Xi

  • Signal Word:No signal word.

  • Hazard Statement:none

  • First-aid measures: General adviceConsult a physician. Show this safety data sheet to the doctor in attendance.If inhaled If breathed in, move person into fresh air. If not breathing, give artificial respiration. Consult a physician. In case of skin contact Wash off with soap and plenty of water. Consult a physician. In case of eye contact Rinse thoroughly with plenty of water for at least 15 minutes and consult a physician. If swallowed Never give anything by mouth to an unconscious person. Rinse mouth with water. Consult a physician. Absorption, Distribution and ExcretionResearch suggests that glutathione is not orally bioactive, and that very little of oral glutathione tablets or capsules is actually absorbed by the body.

  • Fire-fighting measures: Suitable extinguishing media Use water spray, alcohol-resistant foam, dry chemical or carbon dioxide. Wear self-contained breathing apparatus for firefighting if necessary.

  • Accidental release measures: Use personal protective equipment. Avoid dust formation. Avoid breathing vapours, mist or gas. Ensure adequate ventilation. Evacuate personnel to safe areas. Avoid breathing dust. For personal protection see section 8. Prevent further leakage or spillage if safe to do so. Do not let product enter drains. Discharge into the environment must be avoided. Pick up and arrange disposal. Sweep up and shovel. Keep in suitable, closed containers for disposal.

  • Handling and storage: Avoid contact with skin and eyes. Avoid formation of dust and aerosols. Avoid exposure - obtain special instructions before use.Provide appropriate exhaust ventilation at places where dust is formed. For precautions see section 2.2. Store in cool place. Keep container tightly closed in a dry and well-ventilated place.

  • Exposure controls/personal protection:Occupational Exposure limit valuesBiological limit values Handle in accordance with good industrial hygiene and safety practice. Wash hands before breaks and at the end of workday. Eye/face protection Safety glasses with side-shields conforming to EN166. Use equipment for eye protection tested and approved under appropriate government standards such as NIOSH (US) or EN 166(EU). Skin protection Wear impervious clothing. The type of protective equipment must be selected according to the concentration and amount of the dangerous substance at the specific workplace. Handle with gloves. Gloves must be inspected prior to use. Use proper glove removal technique(without touching glove's outer surface) to avoid skin contact with this product. Dispose of contaminated gloves after use in accordance with applicable laws and good laboratory practices. Wash and dry hands. The selected protective gloves have to satisfy the specifications of EU Directive 89/686/EEC and the standard EN 374 derived from it. Respiratory protection Wear dust mask when handling large quantities. Thermal hazards

Supplier and reference price

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  • Manufacture/Brand:Usbiological
  • Product Description:Reduced Glutathione
  • Packaging:1Kit
  • Price:$ 476
  • Delivery:In stock
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  • Manufacture/Brand:Usbiological
  • Product Description:Reduced Glutathione
  • Packaging:1Kit
  • Price:$ 525
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  • Manufacture/Brand:TRC
  • Product Description:Glutathione
  • Packaging:5g
  • Price:$ 65
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  • Manufacture/Brand:TRC
  • Product Description:Glutathione
  • Packaging:25g
  • Price:$ 150
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  • Manufacture/Brand:Tocris
  • Product Description:L-Glutathione reduced ≥98%
  • Packaging:5G
  • Price:$ 45
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  • Manufacture/Brand:TCI Chemical
  • Product Description:Glutathione reduced form >97.0%(T)
  • Packaging:10g
  • Price:$ 51
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  • Manufacture/Brand:TCI Chemical
  • Product Description:Glutathione reduced form >97.0%(T)
  • Packaging:1g
  • Price:$ 13
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  • Manufacture/Brand:Sigma-Aldrich
  • Product Description:L-Glutathione reduced ≥98.0%
  • Packaging:100g
  • Price:$ 498
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  • Manufacture/Brand:Sigma-Aldrich
  • Product Description:Glutathione, Reduced, Free Acid - CAS 70-18-8 - Calbiochem Glutathione, Reduced, Free Acid, CAS 70-18-8, is a tripeptide that serves as an endogenous antioxidant and provides protection against auto-oxidation.
  • Packaging:100 g
  • Price:$ 422.72
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  • Manufacture/Brand:Sigma-Aldrich
  • Product Description:Glutathione United States Pharmacopeia (USP) Reference Standard
  • Packaging:300mg
  • Price:$ 325
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Relevant articles and documentsAll total 90 Articles be found

Fraenkel-Conrat

, p. 2534 (1941)

Rate constant determination for the reaction of hydroxyl and glutathione thiyl radicals with glutathione in aqueous solution

Mezyk, Stephen P.

, p. 8861 - 8866 (1996)

The techniques of pulse radiolysis, laser photolysis, and absorption spectroscopy have been used to investigate the glutathione disulfide radical anion formation over the pH range 7.0-13.0 in aqueous solution. Photolysis of the disulfide anion formed from the one-electron oxidation of reduced glutathione perturbs the disulfide anion/thiyl radical equilibrium, allowing the rate constant for. thiyl radical reaction with glutathione to be uniquely determined from the transient absorption bleach and subsequent pseudo-first-order recovery. These pH-dependent values were combined with measured disulfide equilibrium constants to calculate glutathione radical anion dissociation rate constants. From computer modeling of established mechanisms of the observed disulfide radical anion growths, pH-dependent rate constants for the reaction of hydroxyl radicals with glutathione to produce the thiyl radical were obtained. Utilizing literature ionization constants, values for hydroxyl and thiyl radical reactions with individual glutathione species were determined. The similarity of the measured values over the pH range 10-13 suggests that the rate constants for both the hydroxyl and oxide radical reaction with glutathione are essentially the same. These hydroxyl radical rate constants are contrasted with previously reported values determined using competition kinetics.

Synthesis of novel chiral bis-N-substituted-hydrazinecarboxamide receptors and probing their solution-phase recognition to chiral carboxylic guests by ESI-TOF/MS and tandem ESI-MS

Nour, Hany F.,Golon, Agnieszka,Islam, Tuhidul,Fernández-Lahore, Marcelo,Kuhnert, Nikolai

, p. 11130 - 11137 (2013)

Seven novel bis-N-substituted-hydrazinecarboxamide receptors were synthesized in good to excellent yields by reacting chiral dicarbohydrazides, obtained from commercially available tartaric acid, with substituted aromatic isocyanates. The newly synthesized hydrazinecarboxamides formed structurally unique supramolecular aggregates, which have been confirmed by ESI-TOF/MS and tandem ESI-MS. They also showed molecular recognition to a selection of chiral carboxylic guests and oligopeptides, which mimic the backbone structure of the bacterial cell wall. The structures of the novel compounds were verified by various spectroscopic techniques including FTIR, 1H NMR, 13C NMR, ESI-TOF/MS, tandem ESI-MS, 2D ROESY NMR, and CD spectroscopy.

Convenient supported recyclable material based on dihydrolipoyl-residue for the reduction of disulfide derivatives

Bienvenu, Céline,Greiner, Jacques,Vierling, Pierre,Giorgio, Christophe Di

, p. 3309 - 3311 (2010)

A quantitative method for the reduction of disulfides, which uses a totally recyclable solid phase supported reducing agent, is reported. d,l-α-Lipoic acid was quantitatively condensed on a highly stable 100% PEG Aminomethyl-ChemMatrix resin that can swell in aqueous media as well as in organic solvents. Lipoic residue, subsequently reduced to its dihydrolipoyl form, was utilized as a reducing agent for highly valuable disulfide compounds.

Dissecting the catalytic mechanism of trypanosoma brucei trypanothione synthetase by kinetic analysis and computational modeling

Leroux, Alejandro E.,Haanstra, Jurgen R.,Bakker, Barbara M.,Krauth-Siegel, R. Luise

, p. 23751 - 23764 (2013)

Background: Trypanothione synthetase catalyzes the conjugation of spermidine with two GSH molecules to form trypanothione. Results: The kinetic parameters were measured under in vivo-like conditions. A mathematical model was developed describing the entire kinetic profile. Conclusion: Trypanothione synthetase is affected by substrate and product inhibition. Significance: The combined kinetic and modeling approaches provided a so far unprecedented insight in the mechanism of this parasite-specific enzyme.

Metabolic synthesis of clickable glutathione for chemoselective detection of glutathionylation

Samarasinghe, Kusal T. G.,Munkanatta Godage, Dhanushka N. P.,Vanhecke, Garrett C.,Ahn, Young-Hoon

, p. 11566 - 11569 (2014)

Glutathionylation involves reversible protein cysteine modification that regulates the function of numerous proteins in response to redox stimuli, thereby altering cellular processes. Herein we developed a selective and versatile approach to identifying glutathionylation by using a mutant of glutathione synthetase (GS). GS wild-type catalyzes coupling of γGlu-Cys to Gly to form glutathione. We generated a GS mutant that catalyzes azido-Ala in place of Gly with high catalytic efficiency and selectivity. Transfection of this GS mutant (F152A/S151G) and incubation of azido-Ala in cells efficiently afford the azide-containing glutathione derivative, γGlu-Cys-azido-Ala. Upon H2O2 treatment, clickable glutathione allowed for selective and sensitive detection of glutathionylated proteins by Western blotting or fluorescence after click reaction with biotin-alkyne or rhodamine-alkyne. This approach affords the efficient metabolic tagging of intracellular glutathione with small clickable functionality, providing a versatile handle for characterizing glutathionylation.

Hopkins,Morgan

, (1945)

Kinetic, spectroscopic and in silico characterization of the first step of the reaction between glutathione and selenite

Dereven'kov, Ilia A.,Hannibal, Luciana,Molodtsov, Pavel A.,Branzanic, Adrian M.V.,Silaghi-Dumitrescu, Radu,Makarov, Sergei V.

, (2020)

Reduction of dietary selenite (SeO3H?, SeO3H2) is an important process in vivo, which predominantly involves glutathione (GSH). Although the reaction between selenite and thiols has been studied extensively, its mechanism and the identification of products remain controversial. Herein, we present kinetic, spectroscopic and in silico data on the first step of the reaction between GSH and SeO32? in aqueous solutions of varying acidity. We found that the reaction reversibly produces glutathione-S-selenite (GS-SeO2?) absorbing at 259 nm in the UV spectrum. Assignment of the absorption maximum at 259 nm to GS-SeO2? was performed using TDDFT and mass spectrometry. GS-SeO2? undergoes protonation in acidic medium to form the corresponding conjugated acid, GS-SeO2H (pKa = 1.9 at 25 °C), which exhibits reduced absorption intensity at 259 nm. According to the kinetic data, the mechanism of GS-SeO2?(H+) formation includes two pathways: (i) nucleophilic substitution of HO-group in biselenite by the thiolate group of GSH, and (ii) nucleophilic substitution of HO-group in selenous acid by the thiol group of GSH. The complex GS-SeO2?(H+) is unstable in aqueous medium and undergoes hydrolysis to initial reactants, which is accelerated by an increase in alkalinity.

Millisecond dynamics in glutaredoxin during catalytic turnover is dependent on substrate binding and absent in the resting states

Jensen, Kristine Steen,Winther, Jakob R.,Teilum, Kaare

, p. 3034 - 3042 (2011)

Conformational dynamics is important for enzyme function. Which motions of enzymes determine catalytic efficiency and whether the same motions are important for all enzymes, however, are not well understood. Here we address conformational dynamics in glutaredoxin during catalytic turnover with a combination of NMR magnetization transfer, R2 relaxation dispersion, and ligand titration experiments. Glutaredoxins catalyze a glutathione exchange reaction, forming a stable glutathinoylated enzyme intermediate. The equilibrium between the reduced state and the glutathionylated state was biochemically tuned to exchange on the millisecond time scale. The conformational changes of the protein backbone during catalysis were followed by 15N nuclear spin relaxation dispersion experiments. A conformational transition that is well described by a two-state process with an exchange rate corresponding to the glutathione exchange rate was observed for 23 residues. Binding of reduced glutathione resulted in competitive inhibition of the reduced enzyme having kinetics similar to that of the reaction. This observation couples the motions observed during catalysis directly to substrate binding. Backbone motions on the time scale of catalytic turnover were not observed for the enzyme in the resting states, implying that alternative conformers do not accumulate to significant concentrations. These results infer that the turnover rate in glutaredoxin is governed by formation of a productive enzyme-substrate encounter complex, and that catalysis proceeds by an induced fit mechanism rather than by conformer selection driven by intrinsic conformational dynamics.

Characterization of nucleoside and DNA adducts formed by S-(1-Acetoxymethyl)glutathione and implications for dihalomethane - Glutathione conjugates

Marsch, Glenn A.,Mundkowski, Ralf G.,Morris, Brent J.,Manier, M. Lisa,Hartman, Melanie K.,Guengerich, F. Peter

, p. 600 - 608 (2001)

S-(1-Acetoxymethyl)glutathione (GSCH2OAc) was synthesized and used as a model for the reaction of glutathione (GSH)-dihaloalkane conjugates with nucleosides and DNA. Previously, S-[1-(N2-deoxyguanosinyl)methyl]GSH had been identified as the major adduct formed in the reaction of GSCH2OAc with deoxyguanosine. GSCH2OAc was incubated with the three remaining deoxyribonucleosides to identify other possible adducts. Adducts to all three nucleosides were found using electrospray ionization mass spectrometry (ESI MS). The adduct of GSCH2OAc and deoxyadenosine was formed in yield of up to 0.05% and was identified as S-[1-(N7-deoxyadenosinyl)methyl]GSH. The pyrimidine deoxyribonucleoside adducts were formed more efficiently, resulting in yields of 1 and 2% for the GSCH2OAc adducts derived from thymidine and deoxycytidine, respectively, but their lability prevented their structural identification by 1H NMR. On the basis of the available UV spectra, we propose the structures S-[1-(N3-thymidinyl)methyl]GSH and S-[1-(N4-deoxycytidinyl)methyl]GSH. Because adduct degradation occurred most rapidly at alkaline and neutral pH values, an enzymatic DNA digestion procedure was developed for the rapid hydrolysis of DNA to deoxyribonucleosides at acidic pH. DNA digests were completed in less than 2 h with a two-step method, which consisted of a 15 min incubation of DNA with high concentrations of deoxyribonuclease II and phosphodiesterase II at pH 4.5, followed by incubation of resulting nucleotides with acid phosphatase. Analysis of the hydrolysis products by HPLC-ESI-MS indicated the presence of the thymidine adduct.

A New Synthesis of Glutathione via the Thiazoline Peptide

Ozawa, Yoichi,Tsuji, Toshiaki,Ariyoshi, Yasuo

, p. 2592 - 2593 (1980)

A convenient synthesis of glutathione (GSH) by the use of minimal protecting groups was investigated.N-Formyl-L-2-amino-4-cyanobutyric acid ethyl ester was condensed with ethyl L-cysteinylglycinate to give (4R)-2--4-(ethoxycarbonylmethylcarbamoyl)-2-thiazoline.This compound was saponified in aqueous acetone at -15- -20 deg C and subsequently treated with dilute H2SO4 (pH 4) to yield formylglutathione, whose formyl group was then hydrolyzed with 0.5 M (1M = 1 mol dm-3) H2SO4 to give free GSH.For purification, this was changed to a copper thiolate, which was then decomposed with H2S to afford pure GSH.

Simple single-step single-enzyme synthesis of [14C]-GSH

De Keczer, Steve A.,Voronin, Tatyana,Yao, Jennifer,Zhang, Fang-Jie,Masjedizadeh, Mohammad R.

, p. 110 - 112 (2010)

The tri-peptide [14C]-glutathione ([14C]-GSH) was synthesized in a single step by GSH synthetase catalyzed reaction of L-γ-glutamyl-L-cysteine and [14C]-glycine. Preparative reverse phase HPLC afforded [14C]-GSH in 30% yield and 98% purity. Preparation of GSH synthetase from E. coli via recombinant DNA and the interconversion of [14C]-GSH to the disulfide [14C]-GSSG for storage are discussed. Copyright

Acetone/Isopropanol Photoinitiating System Enables Tunable Disulfide Reduction and Disulfide Mapping via Tandem Mass Spectrometry

Adhikari, Sarju,Yang, Xiaoyue,Xia, Yu

, p. 13036 - 13043 (2018)

Herein, we report the development of a new photochemical system which enables rapid and tunable disulfide bond reduction and its application in disulfide mapping via online coupling with mass spectrometry (MS). Acetone, a clean and electrospray ionization (ESI) compatible solvent, is used as the photoinitiator (1% volume) in the solvent system consisting of 1:1 alkyl alcohol and water. Under ultraviolet (UV) irradiation (~254 nm), the acetone/alcohol system produces hydroxyalkyl radicals, which are responsible for disulfide bond cleavage in peptides. Acetone/isopropanol is most suitable for optimizing the disulfide reduction products, leading to almost complete conversion in less than 5 s when the reaction is conducted in a flow microreactor. The flow microreactor device not only facilitates direct coupling with ESI-MS but also allows fine-tuning of the extent of disulfide reduction by varying the UV exposure time. Near full sequence coverage for peptides consisting of intra- or interchain disulfide bonds has been achieved from complete disulfide reduction and online tandem mass spectrometry (MS/MS) via low energy collision-induced dissociation. Coupling different degrees of partial disulfide reduction with ESI-MS/MS allows disulfide mapping as demonstrated for characterizing the three disulfide bonds in insulin.

Inhibition of thermus thermophilus HB8 thioredoxin activity by platinum(II)

Kato, Masahiro,Yamamoto, Hitoshi,Okamura, Taka-Aki,Maoka, Nobuko,Masui, Ryoji,Kuramitsu, Seiki,Ueyama, Norikazu

, p. 1023 - 1026 (2005)

A 1 : 1 thioredoxin-Pt(bpy) complex 1 was prepared by adding [Pt(bpy)(en)]Cl2 (bpy = 2,2'-bipyridine, en = ethylenediamine) to Thermus thermophilus HB8 thioredoxin in pH 8 phosphate buffer. Matrix-assisted laser desorption-ionization time of flight mass spectrometry (MALDI-TOF MS) and UV spectra of 1 indicate the formation of Pt(bpy)(cys-Ala-Pro-cys-containing peptide fragment). These findings suggest that the Pt(bpy)2+ unit binds to the active site of thioredoxin. The thioredoxin-platinum complex has no catalytic activity for the reduction of glutathione disulfide in the presence of NADPH and thioredoxin reductase, so that the platinum complex functions as an inhibitor. The Royal Society of Chemistry 2005.

Structural and biochemical analyses indicate that a bacterial persulfide dioxygenase-rhodanese fusion protein functions in sulfur assimilation

Motl, Nicole,Skiba, Meredith A.,Kabil, Omer,Smith, Janet L.,Banerjee, Ruma

, p. 14026 - 14038 (2017)

Hydrogen sulfide (H2S) is a signaling molecule that is toxic at elevated concentrations. In eukaryotes, it is cleared via a mitochondrial sulfide oxidation pathway, which comprises sulfide quinone oxidoreductase, persulfide dioxygenase (PDO), rhodanese, and sulfite oxidase and converts H2S to thiosulfate and sulfate. Natural fusions between the non-heme iron containing PDOand rhodanese, a thiol sulfurtransferase, exist in some bacteria. However, little is known about the role of the PDO-rhodanese fusion (PRF) proteins in sulfur metabolism. Herein,we report the kinetic properties and the crystal structure of a PRF from the Gram-negative endophytic bacterium Burkholderia phytofirmans. The crystal structures of wild-type PRF and a sulfurtransferase-inactivated C314S mutant with and without glutathione were determined at 1.8, 2.4, and 2.7 ? resolution, respectively. We found that the two active sites are distant and do not show evidence of direct communication. The B. phytofirmans PRF exhibited robust PDO activity and preferentially catalyzed sulfur transfer in the direction of thiosulfate to sulfite and glutathione persulfide; sulfur transfer in the reverse direction was detectable only under limited turnover conditions. Together with the kinetic data, our bioinformatics analysis reveals that B. phytofirmans PRF is poised to metabolize thiosulfate to sulfite in a sulfur assimilation pathway rather than in sulfide stress response as seen, for example, with the Staphylococcus aureus PRF or sulfide oxidation and disposal as observed with the homologous mammalian proteins.

Adsorption and orientation of the physiological extracellular peptide glutathione disulfide on surface functionalized colloidal alumina particles

Meder, Fabian,Hintz, Henrik,Koehler, Yvonne,Schmidt, Maike M.,Treccani, Laura,Dringen, Ralf,Rezwan, Kurosch

, p. 6307 - 6316 (2013)

Understanding the interrelation between surface chemistry of colloidal particles and surface adsorption of biomolecules is a crucial prerequisite for the design of materials for biotechnological and nanomedical applications. Here, we elucidate how tailoring the surface chemistry of colloidal alumina particles (d50 = 180 nm) with amino (-NH2), carboxylate (-COOH), phosphate (-PO3H2) or sulfonate (-SO3H) groups affects adsorption and orientation of the model peptide glutathione disulfide (GSSG). GSSG adsorbed on native, -NH2-functionalized, and -SO 3H-functionalized alumina but not on -COOH- and -PO3H 2-functionalized particles. When adsorption occurred, the process was rapid (≤5 min), reversible by application of salts, and followed a Langmuir adsorption isotherm dependent on the particle surface functionalization and ζ potential. The orientation of particle bound GSSG was assessed by the release of glutathione after reducing the GSSG disulfide bond and by ζ potential measurements. GSSG is likely to bind via the carboxylate groups of one of its two glutathionyl (GS) moieties onto native and -NH2-modified alumina, whereas GSSG is suggested to bind to -SO3H-modified alumina via the primary amino groups of both GS moieties. Thus, GSSG adsorption and orientation can be tailored by varying the molecular composition of the particle surface, demonstrating a step toward guiding interactions of biomolecules with colloidal particles.

Theoretical and Experimental Investigation of Thermodynamics and Kinetics of Thiol-Michael Addition Reactions: A Case Study of Reversible Fluorescent Probes for Glutathione Imaging in Single Cells

Chen, Jianwei,Jiang, Xiqian,Carroll, Shaina L.,Huang, Jia,Wang, Jin

, p. 5978 - 5981 (2015)

Density functional theory (DFT) was applied to study the thermodynamics and kinetics of reversible thiol-Michael addition reactions. M06-2X/6-31G(d) with the SMD solvation model can reliably predict the Gibbs free energy changes (ΔG) of thiol-Michael addition reactions with an error of less than 1 kcal·mol-1 compared with the experimental benchmarks. Taking advantage of this computational model, the first reversible reaction-based fluorescent probe was developed that can monitor the changes in glutathione levels in single living cells.

Target discovery of ebselen with a biotinylated probe

Chen, Zhenzhen,Jiang, Zhongyao,Chen, Nan,Shi, Qian,Tong, Lili,Kong, Fanpeng,Cheng, Xiufen,Chen, Hao,Wang, Chu,Tang, Bo

, p. 9506 - 9509 (2018)

Despite numerous studies on ebselen over the past decade, its cellular targets remain obscure. Here we synthesized a biotinylated ebselen probe (biotin-ebselen) and characterized ebselen-binding proteins via an efficient activity-based protein profiling (ABPP) method, which allowed for the robust identification of 462 targeted proteins in HeLa cells. This first work of global target profiling of ebselen will be helpful to re-design ebselen-based therapy appropriately in clinical trials.

Reaction of COTC with glutathione: Structure of the putative glyoxalase I inhibitor

Huntley, C. Frederick M.,Hamilton, Diana S.,Creighton, Donald J.,Ganem, Bruce

, p. 3143 - 3144 (2000)

(matrix presented) The structure of the active glyoxalase I inhibitor derived from the Streptomyces griseosporeus metabolite COTC 1 has been conclusively identified by means of total synthesis as 2c. Human glyoxalase I is competitively inhibited by 2c (Ki = 183 ± 6 μM) but is not inhibited by 1 itself.

Development and application of organic reagents for analysis. VIII. Determination of biological thiols with a new fluorogenic thiol-selective reagent, N-(p-[2-(6-dimethylamino)benzofuranyl]phenyl)maleimide.

Nakashima,Nishida,Nakatsuji,Akiyama

, p. 1678 - 1683 (1986)

-

A promiscuous glutathione transferase transformed into a selective thiolester hydrolase

Hederos, Sofia,Tegler, Lotta,Carlsson, Jonas,Persson, Bengt,Viljanen, Johan,Broo, Kerstin S.

, p. 90 - 97 (2006)

Human glutathione transferase A1-1 (hGST A1-1) can be reengineered by rational design into a catalyst for thiolester hydrolysis with a catalytic proficiency of 1.4 × 107 M-1. The thiolester hydrolase, A216H that was obtained by the introduction of a single histidine residue at position 216 catalyzed the hydrolysis of a substrate termed GSB, a thiolester of glutathione and benzoic acid. Here we investigate the substrate requirements of this designed enzyme by screening a thiolester library. We found that only two thiolesters out of 18 were substrates for A216H. The A216H-catalyzed hydrolysis of GS-2 (thiolester of glutathione and naphthalenecarboxylic acid) exhibits a kcat of 0.0032 min -1 and a KM of 41 M. The previously reported catalysis of GSB has a kcat of 0.00078 min-1 and KM of 5 M. The kcat for A216H-catalyzed hydrolysis of GS-2 is thus 4.1 times higher than for GSB. The catalytic proficiency (kcat/K M)/kuncat for GS-2 is 3 × 106 M -1. The promiscuous feature of the wt protein towards a range of different substrates has not been conserved in A216H but we have obtained a selective enzyme with high demands on the substrate. The Royal Society of Chemistry 2006.

The thioredoxin-thioredoxin reductase system can function in vivo as an alternative system to reduce oxidized glutathione in Saccharomyces cerevisiae

Tan, Shi-Xiong,Greetham, Darren,Raeth, Sebastian,Grant, Chris M.,Dawes, Ian W.,Perrone, Gabriel G.

, p. 6118 - 6126 (2010)

Cellular mechanisms that maintain redox homeostasis are crucial, providing buffering against oxidative stress. Glutathione, the most abundant low molecular weight thiol, is considered the major cellular redox buffer in most cells. To better understand how cells maintain glutathione redox homeostasis, cells of Saccharomyces cerevisiae were treated with extracellular oxidized glutathione (GSSG), and the effect on intracellular reduced glutathione (GSH) and GSSG were monitored over time. Intriguingly cells lacking GLR1 encoding the GSSG reductase in S. cerevisiae accumulated increased levels of GSH via a mechanism independent of the GSH biosynthetic pathway. Furthermore, residual NADPH-dependent GSSG reductase activity was found in lysate derived from glr1 cell. The cytosolic thioredoxin-thioredoxin reductase system and not the glutaredoxins (Grx1p, Grx2p, Grx6p, and Grx7p) contributes to the reduction of GSSG. Overexpression of the thioredoxins TRX1 or TRX2 in glr1 cells reduced GSSG accumulation, increased GSH levels, and reduced cellular glutathione E h′. Conversely, deletion of TRX1 or TRX2 in the glr1 strain led to increased accumulation of GSSG, reduced GSH levels, and increased cellular Eh′. Furthermore, it was found that purified thioredoxins can reduce GSSG to GSH in the presence of thioredoxin reductase and NADPH in a reconstituted in vitro system. Collectively, these data indicate that the thioredoxin-thioredoxin reductase system can function as an alternative system to reduce GSSG in S. cerevisiae in vivo.

Electrical 'Wiring' of Glutathione Reductase: an Efficient Method for the Reduction of Glutathione using Molecular Hydrogen as the Reductant

Willner, Itamar,Lapidot, Noa

, p. 617 - 618 (1991)

The enzyme glutathione reductase is chemically modified to become electrically conductive, thus facilitating the reduction of oxidized glutathione to its reduced form using hydrogen as the reductant, and the modified enzyme and Pt colloid as catalysts.

The chemical basis of thiol addition to nitro-conjugated linoleic acid, a protective cell-signaling lipid

Turell, Lucía,Vitturi, Darío A.,Coiti?o, E. Laura,Lebrato, Lourdes,M?ller, Matías N.,Sagasti, Camila,Salvatore, Sonia R.,Woodcock, Steven R.,Alvarez, Beatriz,Schopfer, Francisco J.

, p. 1145 - 1159 (2017)

Nitroalkene fatty acids are formed in vivo and exert protective and anti-inflammatory effects via reversible Michael addition to thiol-containing proteins in key signaling pathways. Nitro-conjugated linoleic acid (NO2-CLA) is preferentially formed, constitutes the most abundant nitrated fatty acid in humans, and contains two carbons that could potentially react with thiols, modulating signaling actions and levels. In this work, we examined the reactions of NO2-CLA with low molecular weight thiols (glutathione, cysteine, homocysteine, cysteinylglycine, and β-mercaptoethanol) and human serum albumin. Reactions followed reversible biphasic kinetics, consistent with the presence of two electrophilic centers in NO2-CLA located on the β- and δ-carbons with respect to the nitro group. The differential reactivity was confirmed by computational modeling of the electronic structure. The rates (kon and koff) and equilibrium constants for both reactions were determined for different thiols. LC-UV-Visible and LC-MS analyses showed that the fast reaction corresponds to β-adduct formation (the kinetic product), while the slow reaction corresponds to the formation of the δ-adduct (the thermodynamic product). The pH dependence of the rate constants, the correlation between intrinsic reactivity and thiol pKa, and the absence of deuterium solvent kinetic isotope effects suggested stepwise mechanisms with thiolate attack on NO2-CLA as rate-controlling step. Computational modeling supported the mechanism and revealed additional features of the transition states, anionic intermediates, and final neutral products. Importantly, the detection of cysteine-δ-adducts in human urine provided evidence for the biological relevance of this reaction. Finally, human serum albumin was found to bind NO2-CLA both non-covalently and to form covalent adducts at Cys-34, suggesting potential modes for systemic distribution. These results provide new insights into the chemical basis of NO2-CLA signaling actions.

Metal-dependent inhibition of glyoxalase II: A possible mechanism to regulate the enzyme activity

Campos-Bermudez, Valeria A.,Morán-Barrio, Jorgelina,Costa-Filho, Antonio J.,Vila, Alejandro J.

, p. 726 - 731 (2010)

Glyoxalase II (GLX2, EC 3.1.2.6., hydroxyacylglutathione hydrolase) is a metalloenzyme involved in crucial detoxification pathways. Different studies have failed in identifying the native metal ion of this enzyme, which is expressed with iron, zinc and/or manganese. Here we report that GloB, the GLX2 from Salmonella typhimurium, is differentially inhibited by glutathione (a reaction product) depending on the bound metal ion, and we provide a structural model for this inhibition mode. This metal-dependent inhibition was shown to occur in metal-enriched forms of the enzyme, complementing the spectroscopic data. Based on the high levels of free glutathione in the cell, we suggest that the expression of the different metal forms of GLX2 during Salmonella infection could be exploited as a mechanism to regulate the enzyme activity.

Thiolation and Carboxylation of Glutathione Synergistically Enhance Its Lead-Detoxification Capabilities

Sauser, Luca,Mohammed, Tagwa A.,Kalvoda, Tadeá?,Feng, Sheng-Jan,Spingler, Bernhard,Rulí?ek, Lubomír,Shoshan, Michal S.

supporting information, p. 18620 - 18624 (2021/12/13)

The natural tripeptide glutathione (GSH) is a ubiquitous compound harboring various biological tasks, among them interacting with essential and toxic metal ions. Yet, although weakly binding the poisonous metal lead (Pb), GSH poorly detoxifies it. β-Mercaptoaspartic acid is a new-to-nature novel amino acid that was found to enhance the Pb-detoxification capability of a synthetic cyclic tetrapeptide. Aiming to explore the advantages of noncanonical amino acids (ncAAs) of this nature, we studied the detoxification capabilities of GSH and three analogue peptides, each of which contains at least one ncAA that harbors both free carboxylate and thiolate groups. A thorough investigation that includes in vitro detoxification and mechanistic evaluations, metal-binding affinity, metal selectivity, and computational studies shows that these ncAAs are highly beneficial in additively enhancing Pb binding and reveals the importance of both high affinity and metal selectivity in synergistically reducing Pb toxicity in cells. Hence, such ncAAs join the chemical toolbox against Pb poisoning and pollution, enabling peptides to strongly and selectively bind the toxic metal ion.

Visible Light-Mediated Synthesis of Se?S Bond-Containing Peptides

Arsenyan, Pavel,Dimitrijevs, Pavels,Lapcinska, Sindija

supporting information, p. 3968 - 3972 (2021/07/26)

A visible light-initiated method has been developed for preparation of Se?S bond-containing peptides. The method is based on generation of sulfur-centered radical employing organic dye. The protocol is tolerant to unprotected peptides with “sensitive” amino acids. The stability of Se?S bond is evaluated in buffers at different pH (3.0–10.0) and also in the presence of oxidants and reducing agents. Additionally, the ability of Se?S bond to serve as an oxidation sensitive linker in biocompatible materials has been confirmed. (Figure presented.).

Ethynylation of Cysteine Residues: From Peptides to Proteins in Vitro and in Living Cells

Tessier, Romain,Nandi, Raj Kumar,Dwyer, Brendan G.,Abegg, Daniel,Sornay, Charlotte,Ceballos, Javier,Erb, Stéphane,Cianférani, Sarah,Wagner, Alain,Chaubet, Guilhem,Adibekian, Alexander,Waser, Jerome

supporting information, p. 10961 - 10970 (2020/05/18)

Current approaches to introduce terminal alkynes for bioorthogonal reactions into biomolecules still present limitations in terms of either reactivity, selectivity, or adduct stability. We present a method for the ethynylation of cysteine residues based on the use of ethynylbenziodoxolone (EBX) reagents. The acetylene group is directly introduced onto the thiol group of cysteine and can be used for copper-catalyzed alkyne-azide cycloaddition (CuAAC) without further processing. Labeling proceeded with reaction rates comparable to or higher than the most often used iodoacetamide on peptides or maleimide on the antibody trastuzumab, and high cysteine selectivity was observed. The reagents were also used in living cells for cysteine proteomic profiling and displayed improved coverage of the cysteinome compared to previously reported iodoacetamide or hypervalent iodine reagents. Fine-tuning of the EBX reagents allows optimization of their reactivity and physical properties.

Crystal-facet-dependent denitrosylation: Modulation of NO release from S-nitrosothiols by Cu2O polymorphs

Ghosh, Sourav,Roy, Punarbasu,Prasad, Sanjay,Mugesh, Govindasamy

, p. 5308 - 5318 (2019/05/29)

Nitric oxide (NO), a gaseous small molecule generated by the nitric oxide synthase (NOS) enzymes, plays key roles in signal transduction. The thiol groups present in many proteins and small molecules undergo nitrosylation to form the corresponding S-nitrosothiols. The release of NO from S-nitrosothiols is a key strategy to maintain the NO levels in biological systems. However, the controlled release of NO from the nitrosylated compounds at physiological pH remains a challenge. In this paper, we describe the synthesis and NO releasing ability of Cu2O nanomaterials and provide the first experimental evidence that the nanocrystals having different crystal facets within the same crystal system exhibit different activities toward S-nitrosothiols. We used various imaging techniques and time-dependent spectroscopic measurements to understand the nature of catalytically active species involved in the surface reactions. The denitrosylation reactions by Cu2O can be carried out multiple times without affecting the catalytic activity.

Process route upstream and downstream products

Process route

(S)-2-Amino-4-[(R)-1-(carboxymethyl-carbamoyl)-2-(hydroxy-phenyl-methylsulfanyl)-ethylcarbamoyl]-butyric acid

(S)-2-Amino-4-[(R)-1-(carboxymethyl-carbamoyl)-2-(hydroxy-phenyl-methylsulfanyl)-ethylcarbamoyl]-butyric acid

GLUTATHIONE
70-18-8

GLUTATHIONE

benzaldehyde
100-52-7

benzaldehyde

Conditions
Conditions Yield
In water; at 25 ℃; Equilibrium constant;
<i>L</i>-γ-glutamyl-><i>S</i>-((1Ξ,2Ξ)-1,2-dihydroxy-3-phosphonooxy-propyl)-<i>L</i>-cysteinyl->glycine

L-γ-glutamyl->S-((1Ξ,2Ξ)-1,2-dihydroxy-3-phosphonooxy-propyl)-L-cysteinyl->glycine

DL-glyceraldehyde 3-phosphate
142-10-9,591-57-1,20283-52-7,591-59-3

DL-glyceraldehyde 3-phosphate

GLUTATHIONE
70-18-8

GLUTATHIONE

Conditions
Conditions Yield
In water; at 25 ℃; Equilibrium constant;
Oxidized glutathione
27025-41-8,121-24-4,87140-29-2

Oxidized glutathione

L-Cysteine
52-90-4

L-Cysteine

GLUTATHIONE
70-18-8

GLUTATHIONE

N<SUP>5</SUP>-((R)-3-(((R)-2-amino-2-carboxyethyl)disulfanyl)-1-((carboxymethyl)amino)-1-oxopropan-2-yl)-L-glutamine
13081-14-6

N5-((R)-3-(((R)-2-amino-2-carboxyethyl)disulfanyl)-1-((carboxymethyl)amino)-1-oxopropan-2-yl)-L-glutamine

Conditions
Conditions Yield
With sodium chloride; In water-d2; at 25 ℃; Equilibrium constant;
With sodium chloride; In water-d2; at 25 ℃; Rate constant; Equilibrium constant; various pD values;
(S)-5-((R)-3-(2-naphthoylthio)-1-(carboxymethylamino)-1-oxopropan-2-ylamino)-2-amino-5-oxopentanoic acid

(S)-5-((R)-3-(2-naphthoylthio)-1-(carboxymethylamino)-1-oxopropan-2-ylamino)-2-amino-5-oxopentanoic acid

GLUTATHIONE
70-18-8

GLUTATHIONE

naphthalene-2-carboxylate
93-09-4

naphthalene-2-carboxylate

Conditions
Conditions Yield
With thiolester hydrolase A216H; at 25 ℃; pH=7; Enzyme kinetics;
C<sub>16</sub>H<sub>22</sub>N<sub>4</sub>O<sub>7</sub>S

C16H22N4O7S

GLUTATHIONE
70-18-8

GLUTATHIONE

Nitrosobenzene
586-96-9

Nitrosobenzene

Conditions
Conditions Yield
In water; acetonitrile; at 25 ℃; Equilibrium constant; Rate constant;
C<sub>17</sub>H<sub>24</sub>N<sub>4</sub>O<sub>7</sub>S

C17H24N4O7S

GLUTATHIONE
70-18-8

GLUTATHIONE

3-nitrosotoluene
620-26-8

3-nitrosotoluene

Conditions
Conditions Yield
In water; acetonitrile; at 25 ℃; Equilibrium constant; Rate constant; pH 7.49;
S-(N-benzylthiocarbamoyl)glutathione

S-(N-benzylthiocarbamoyl)glutathione

GLUTATHIONE
70-18-8

GLUTATHIONE

Benzyl isothiocyanate
622-78-6

Benzyl isothiocyanate

Conditions
Conditions Yield
In water; dimethyl sulfoxide; at 37 ℃; pH=7.4; Further Variations:; pH-values; Kinetics; Product distribution;
C<sub>17</sub>H<sub>24</sub>N<sub>4</sub>O<sub>7</sub>S

C17H24N4O7S

GLUTATHIONE
70-18-8

GLUTATHIONE

1-methyl-4-nitrosobenzene
623-11-0

1-methyl-4-nitrosobenzene

Conditions
Conditions Yield
In water; acetonitrile; at 25 ℃; Equilibrium constant; Rate constant; pH 7.49;
methylmercury-L-glutathionate

methylmercury-L-glutathionate

1-(2-hydroxyethyl)-3-methyl-1H-benzo[d]imidazole-2(3H)-thione

1-(2-hydroxyethyl)-3-methyl-1H-benzo[d]imidazole-2(3H)-thione

GLUTATHIONE
70-18-8

GLUTATHIONE

mercury sulfide

mercury sulfide

dimethylmercury
593-74-8

dimethylmercury

1-(2-hydroxyethyl)-3-methyl-1H-benzo[d]imidazol-2(3H)-one
2033-53-6

1-(2-hydroxyethyl)-3-methyl-1H-benzo[d]imidazol-2(3H)-one

Conditions
Conditions Yield
methylmercury-L-glutathionate; 1-(2-hydroxyethyl)-3-methyl-1H-benzo[d]imidazole-2(3H)-thione; In water; acetonitrile; at 37 ℃; for 1h;
With sodium hydrogencarbonate; In water; acetonitrile; at 37 ℃; for 5h;
40%
11 mg
methylmercury-L-glutathionate

methylmercury-L-glutathionate

1-(2-hydroxyethyl)-3-methyl-1H-benzo[d]imidazole-2(3H)-selenone

1-(2-hydroxyethyl)-3-methyl-1H-benzo[d]imidazole-2(3H)-selenone

GLUTATHIONE
70-18-8

GLUTATHIONE

HgSSe

HgSSe

dimethylmercury
593-74-8

dimethylmercury

1-(2-hydroxyethyl)-3-methyl-1H-benzo[d]imidazol-2(3H)-one
2033-53-6

1-(2-hydroxyethyl)-3-methyl-1H-benzo[d]imidazol-2(3H)-one

Conditions
Conditions Yield
methylmercury-L-glutathionate; 1-(2-hydroxyethyl)-3-methyl-1H-benzo[d]imidazole-2(3H)-selenone; In water; acetonitrile; at 37 ℃; for 1h;
With sodium hydrogencarbonate; In water; acetonitrile; at 37 ℃; for 5h;
14 mg

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