2-(S-谷胱甘酰)氢醌 | 76726-99-3

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 中文名称: 2-(S-谷胱甘酰)氢醌
• 英文名称: 2-(Glutathio-S-yl)-1,4-hydroquinone
• 英文别名: (glutathion-S-yl)-1,4-hydroquinone；S-glutathionyl-p-benzohydroquinone；2-(L-glutathion-S-yl)hydroquinone；S-glutathionyl-p-hydroquinone；2-(S-Glutathionyl)hydroquinone；(2S)-2-amino-5-[[(2R)-1-(carboxymethylamino)-3-(2,5-dihydroxyphenyl)sulfanyl-1-oxopropan-2-yl]amino]-5-oxopentanoic acid
• CAS: 76726-99-3
• 化学式: C₁₆H₂₁N₃O₈S
• 分子量: 415.424
• InChiKey: PBSYQNUIZQXWAE-UWVGGRQHSA-N

物化性质

• 沸点：
  887.8±65.0 °C(Predicted)
• 密度：
  1.57±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -3.3
• 重原子数：
  28
• 可旋转键数：
  11
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  225
• 氢给体数：
  7
• 氢受体数：
  10

反应信息

• 作为反应物：
  描述：

  2-(S-谷胱甘酰)氢醌 在 甲酸 、 三氯化铁 作用下， 生成 (glutathion-S-yl)-1,4-benzoquinone
  参考文献：
  名称：

  谷胱甘肽的α-氨基的环加成增加了苯醌硫醚的反应性。

  摘要：

  发现2-（谷胱甘肽-S-基）-1，4-苯醌在磷酸盐缓冲液（pH 7.4）中即使在没有氧气的情况下也明显不稳定。谷氨酸残基的α-氨基分子内加到醌环上最终产生2，3-（谷胱甘肽-N，S-基）-1，4-苯醌和2，6-（谷胱甘肽-N，S-基） ）-1,4-苯醌与3：2-（谷胱甘肽-S-基）-1,4-氢醌的比例为3：1。动力学研究表明，环化反应以k1为0.093 min-1的速率进行，而分子间反应遵循二级动力学，k2为94 M-1 min-1（pH 7.4，37摄氏度），从而导致多重聚合产品。2-（谷胱甘肽-S-基）-1,4-苯醌的两个分子内氨基加合物都易于水解，导致在环中插入一个额外的OH基。这些S-取代的三羟基苯衍生物特别容易自氧化。已显示模型化合物6-（N-乙酰基半胱氨酸-S-基）-2-羟基-1,4-氢醌在自氧化时容易形成两个阻转异构联苯：2,4'-双（N-乙酰基半胱氨酸-S-基） -2'，3

  DOI：

  10.1021/tx9800699
• 作为产物：
  描述：

  谷胱甘肽 、 对苯醌 在 乙二胺四乙酸 、 三羟甲基氨基甲烷盐酸盐 作用下， 以 水 为溶剂， 生成 2-(S-谷胱甘酰)氢醌
  参考文献：
  名称：

  Glutathione Transferases of Phanerochaete chrysosporium

  摘要：

  The white rot fungus Phanerochaete chrysosporium, a saprophytic basidiomycete, possesses a large number of cytosolic glutathione transferases, eight of them showing similarity to the Omega class. PcGSTO1 (subclass I, the bacterial homologs of which were recently proposed, based on their enzymatic function, to constitute a new class of glutathione transferase named S-glutathionyl-(chloro)hydroquinone reductases) and PcGSTO3 (subclass II related to mammalian homologs) have been investigated in this study. Biochemical investigations demonstrate that both enzymes are able to catalyze deglutathionylation reactions thanks to the presence of a catalytic cysteinyl residue. This reaction leads to the formation of a disulfide bridge between the conserved cysteine and the removed glutathione from their substrate. The substrate specificity of each isoform differs. In particular PcGSTO1, in contrast to PcGSTO3, was found to catalyze deglutathionylation of S-glutathionyl-p-hydroquinone substrates. The three-dimensional structure of PcGSTO1 presented here confirms the hypothesis that it belongs not only to a new biological class but also to a new structural class that we propose to name GST xi. Indeed, it shows specific features, the most striking ones being a new dimerization mode and a catalytic site that is buried due to the presence of long loops and that contains the catalytic cysteine.

  DOI：

  10.1074/jbc.m110.194548

文献信息

• Determination of Reduced Cysteine in Oenological Cell Wall Fractions of <i>Saccharomyces cerevisiae</i>
  作者：Antonio Tirelli、Daniela Fracassetti、Ivano De Noni

  DOI：10.1021/jf904047u

  日期：2010.4.28

  Compounds containing cysteine residues, such as glutathione, can affect the redox potential of must and wine by reduction of o-quinones and hydrogen peroxide. The oenological yeast cell wall fractions contain cysteine residues in their protein structure, and they could affect both oxidative and odor properties of wine. An analytical approach based on the derivatization of cysteinyl residues with p-benzoquinone followed by reversed-phase high-performance liquid chromatography separation was developed to quantify glutathione and free and protein cysteine in 16 Saccharomyces cerevisiae strains and 12 commercial samples of yeast mannoproteins, hulls, and lysates. The chemical modifications induced by the Mail lard reaction following the industrial preparation of such fractions were evaluated as well. Lysates showed the highest protein cysteine content and high contents of glutathione and free cysteine. Mannoproteins showed an intense Mail lard reaction (furosine >60 mg/100 g protein), and most of the samples were able to bind thiol compounds with a potentially detrimental effect toward the thiol-related odors in wine.
• Covalent Protein Adducts of Hydroquinone in Tissues from Rats:  Identification and Quantitation of Sulfhydryl-Bound Forms
  作者：Rodney J. Boatman、J. Caroline English、Louise G. Perry、Laurie A. Fiorica

  DOI：10.1021/tx000037x

  日期：2000.9.1

  The Michael-type addition of sulfhydryl groups to benzoquinone (BQ) or substituted benzoquinones is proposed as the primary mechanism by which these electrophilic intermediates react with either cellular glutathione or protein sulfhydryls. This reaction constitutes a reductive alkylation with a substituted hydroquinone (HQ) derivative resulting from the addition. In the case of HQ, oxidative conversion of the parent material to BQ followed by conjugation with glutathione leads to metabolic activation, producing intermediates which are nephrotoxic as well as having other proposed biological activities. Chemically, BQ may react with more than 1 equiv of glutathione (or other sulfhydryl reagents) to produce HQ derivatives substituted with up to four sulfhydryl groups. Similarly, multiply substituted protein-S adducts of HQ were anticipated to occur in vivo following administration of this material. In the current studies, sulfhydryl-bound HQ protein adducts were detected and quantitated in protein isolated from rats using a modification of the alkaline permethylation procedure of Slaughter and Hanzlik [(1993) Anal. Biochem. 208, 288-295]. In particular, total protein-S adducts to HQ in kidney or blood reached a level of 420 or 80 pmol/mg of protein, respectively, 6 h following a single gavage dose of 100 mg/kg HQ. Measured half-lives of protein-S adducts in kidney and blood were 23.9 and 36.0 h, respectively. The applicability of protein-S adducts as a tissue dosimeter for HQ is discussed.
• Alkylation of Cytochrome <i>c</i> by (Glutathion-<i>S</i>-yl)-1,4-benzoquinone and Iodoacetamide Demonstrates Compound-Dependent Site Specificity
  作者：Maria D. Person、Daniel E. Mason、Daniel C. Liebler、Terrence J. Monks、Serrine S. Lau

  DOI：10.1021/tx049873n

  日期：2005.1.1

  The reaction of cytochrome c with the electrophilic compounds (glutathion-S-yl)-1,4-benzoquinone (GSBQ) and iodoacetamide was studied using mass spectrometry. GSBQ is a nephrotoxic quinol-thioether metabolite of benzoquinone, while iodoacetamide is an alkylating agent targeting cysteine thiols. Both chemicals formed covalent adducts with cytochrome c. GSBQ formed adducts with cytochrome c at pH 6 on several histidine and lysine residues. At a pH > 7, the initial product rearranged to a disubstituted cyclic quinone species preferentially found at two sites on the protein, Lys25-Lys27 and Lys86-Lys87, via quinol amine linkages. These two sites were previously determined to be the targets of benzoquinone adduct formation [Person et al. (2003) Chem. Res. Toxicol. 16, 598-608]. Cyclic reaction products are preferentially formed at two sites on the protein because of the presence of multiple basic residues in a conformationally flexible region whereas noncyclic products bind to a broad spectrum of available lysine and histidine nucleophiles. Iodoacetamide was a less selective alkylating agent able to form adducts on the majority of the nucleophilic sites of the protein. MS/MS spectra were used to identify signature ions for GSBQ-adducted peptides from the characteristic fragmentation patterns. Neutral losses of the 129 Da gamma-glutamate residue and of the 273 Da glutathione moiety were found in both cysteine thiol- and lysine amine-linked GSBQ adduct MS/MS. Characteristic fragment ions were used in conjunction with the scoring algorithm for spectral analysis to search for adducted species present at low levels in the sample, and the analysis is applicable generally to detection of glutathione conjugates by MS/MS. Parallel analysis using matrix-assisted laser desorption/ionization-MS to compare spectra of control and treated samples allowed identification of peptide adducts formed by direct addition of GSBQ and by the subsequent loss of the glutathione moiety in a pH-dependent cyclization reaction.
• Glutathione Transferases of Phanerochaete chrysosporium
  作者：Edgar Meux、Pascalita Prosper、Andrew Ngadin、Claude Didierjean、Mélanie Morel、Stéphane Dumarçay、Tiphaine Lamant、Jean-Pierre Jacquot、Frédérique Favier、Eric Gelhaye

  DOI：10.1074/jbc.m110.194548

  日期：2011.3

  The white rot fungus Phanerochaete chrysosporium, a saprophytic basidiomycete, possesses a large number of cytosolic glutathione transferases, eight of them showing similarity to the Omega class. PcGSTO1 (subclass I, the bacterial homologs of which were recently proposed, based on their enzymatic function, to constitute a new class of glutathione transferase named S-glutathionyl-(chloro)hydroquinone reductases) and PcGSTO3 (subclass II related to mammalian homologs) have been investigated in this study. Biochemical investigations demonstrate that both enzymes are able to catalyze deglutathionylation reactions thanks to the presence of a catalytic cysteinyl residue. This reaction leads to the formation of a disulfide bridge between the conserved cysteine and the removed glutathione from their substrate. The substrate specificity of each isoform differs. In particular PcGSTO1, in contrast to PcGSTO3, was found to catalyze deglutathionylation of S-glutathionyl-p-hydroquinone substrates. The three-dimensional structure of PcGSTO1 presented here confirms the hypothesis that it belongs not only to a new biological class but also to a new structural class that we propose to name GST xi. Indeed, it shows specific features, the most striking ones being a new dimerization mode and a catalytic site that is buried due to the presence of long loops and that contains the catalytic cysteine.
• Ring Addition of the α-Amino Group of Glutathione Increases the Reactivity of Benzoquinone Thioethers
  作者：Carmen Alt、Peter Eyer

  DOI：10.1021/tx9800699

  日期：1998.10.1

  sequence of glutathione S-addition, followed by oxidation, N-addition, oxidation, and hydrolysis, constitutes a novel and very effective activation pathway of quinones for eliciting oxidative stress. These data underline the fact that glutathione conjugates of autoxidizable aromatics are no obligatory stable end products of a detoxication reaction. The possible toxicological impacts of intra- and intermolecular

  发现2-（谷胱甘肽-S-基）-1，4-苯醌在磷酸盐缓冲液（pH 7.4）中即使在没有氧气的情况下也明显不稳定。谷氨酸残基的α-氨基分子内加到醌环上最终产生2，3-（谷胱甘肽-N，S-基）-1，4-苯醌和2，6-（谷胱甘肽-N，S-基） ）-1,4-苯醌与3：2-（谷胱甘肽-S-基）-1,4-氢醌的比例为3：1。动力学研究表明，环化反应以k1为0.093 min-1的速率进行，而分子间反应遵循二级动力学，k2为94 M-1 min-1（pH 7.4，37摄氏度），从而导致多重聚合产品。2-（谷胱甘肽-S-基）-1,4-苯醌的两个分子内氨基加合物都易于水解，导致在环中插入一个额外的OH基。这些S-取代的三羟基苯衍生物特别容易自氧化。已显示模型化合物6-（N-乙酰基半胱氨酸-S-基）-2-羟基-1,4-氢醌在自氧化时容易形成两个阻转异构联苯：2,4'-双（N-乙酰基半胱氨酸-S-基） -2'，3