(glutathion-S-yl)-1,4-benzoquinone | 125409-88-3

• 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
• 英文名称: (glutathion-S-yl)-1,4-benzoquinone
• 英文别名: 2-(Glutathio-S-yl)-1,4-benzoquinone；2-(glutathion-S-yl)-1,4-benzoquinone；(2S)-2-amino-5-[[(2R)-1-(carboxymethylamino)-3-(3,6-dioxocyclohexa-1,4-dien-1-yl)sulfanyl-1-oxopropan-2-yl]amino]-5-oxopentanoic acid
• CAS: 125409-88-3
• 化学式: C₁₆H₁₉N₃O₈S
• 分子量: 413.408
• InChiKey: AXIZSDLVOLLWID-UWVGGRQHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -4.3
• 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：
  218
• 氢给体数：
  5
• 氢受体数：
  10

反应信息

• 作为反应物：
  描述：

  (glutathion-S-yl)-1,4-benzoquinone 、 AGAGCAGAG 以 水 为溶剂， 反应 1.5h， 生成
  参考文献：
  名称：

  Alkylation of Cytochrome c by (Glutathion-S-yl)-1,4-benzoquinone and Iodoacetamide Demonstrates Compound-Dependent Site Specificity

  摘要：

  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.

  DOI：

  10.1021/tx049873n
• 作为产物：
  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