SeH(1-) | 16661-43-1

• 分子结构分类: 无机化合物 - 均质非金属化合物 - 其他非金属有机物
• 英文名称: SeH(1-)
• 英文别名: Selanide
• CAS: 16661-43-1
• 化学式: HSe
• 分子量: 79.9679
• InChiKey: SPVXKVOXSXTJOY-UHFFFAOYSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  -0.65
• 重原子数：
  1
• 可旋转键数：
  0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  0
• 氢给体数：
  0
• 氢受体数：
  1

反应信息

• 作为反应物：
  描述：

  SeH(1-) 在 N,N-dimethyl-4-nitrosoaniline 作用下， 以 further solvent(s) 为溶剂， 生成 selenium
  参考文献：
  名称：

  Redox reactions of hydrogen selenide ion

  摘要：

  DOI：

  10.1016/s0020-1693(00)80061-4
• 作为产物：
  描述：

  selenium 在 DL-dithiothreitol 作用下， 以 not given 为溶剂， 生成 SeH(1-)
  参考文献：
  名称：

  Redox reactions of hydrogen selenide ion

  摘要：

  DOI：

  10.1016/s0020-1693(00)80061-4
• 作为试剂：
  描述：

  1,3-二甲基苯并咪唑-2-硫酮 在 SeH(1-) 作用下， 以 乙醇 为溶剂， 生成 1,3-dimethylbenzimidazole-2-selenone
  参考文献：
  名称：

  Cristiani, Franco; Devillanova, Francesco A.; Diaz, Angelo, Phosphorus and Sulfur and the Related Elements, 1984, vol. 20, p. 231 - 240

  摘要：

  DOI：

文献信息

• On the Constituents of Aqueous Polyselenide Electrolytes: A Combined Theoretical and Raman Spectroscopic Study
  作者：A. Goldbach、J. Johnson、D. Meisel、L. A. Curtiss、Marie-Louise Saboungi

  DOI：10.1021/ja9836186

  日期：1999.5.1

  speciation of aqueous polyselenide solutions at high pH values has been investigated by Raman and UV/vis absorption spectroscopy. Complementary, ab initio molecular orbital calculations at the HF/6-31+G* level of theory have been carried out on the vibrational frequencies of polyselenide dianions Sex2- (x = 2−4), polyselenide radical anions Sex- (x = 2, 3), and protonated polyselenides HSex- (x = 1−3) in

  已通过拉曼和紫外/可见吸收光谱研究了高 pH 值下聚硒化物水溶液的形态。已经对聚硒化物二价阴离子 Sex2- (x = 2−4)、聚硒化物自由基阴离子 Sex- (x = 2) 的振动频率在 HF/6-31+G* 理论水平上进行了互补的、从头算分子轨道计算, 3) 和质子化聚硒化物 HSex- (x = 1−3) 以证实实验拉曼光谱的分配。尽管光谱表明随着溶液的逐渐氧化，Se22-、Se32- 和 Se42- 相继形成，但在 269 和 324 cm-1 处仅观察到两个特征拉曼谱带。在用蓝光激发后观察到 269 cm-1 波段的一系列泛音。同样在用绿光激发后出现 324 cm-1 波段的强泛音。269 cm-1 特征归于 Se42-，而 324 cm-1 谱带归于自由基阴离子 Se2-。水中聚硒自由基的发生...
• Synthesis of 5-methylaminomethyl-2-selenouridine in tRNAs: 31P NMR studies show the labile selenium donor synthesized by the selD gene product contains selenium bonded to phosphorus.
  作者：Z Veres、L Tsai、T D Scholz、M Politino、R S Balaban、T C Stadtman

  DOI：10.1073/pnas.89.7.2975

  日期：1992.4

  An enzyme preparation from Salmonella typhimurium catalyzes the conversion of 5-methylaminomethyl-2-thiouridine in tRNAs to 5-methylaminomethyl-2-selenouridine when supplemented with selenide and ATP. Similar preparations from a Salmonella mutant strain carrying a defective selD gene fail to catalyze this selenium substitution reaction. However, supplementation of the deficient enzyme preparation with the purified selD gene product (SELD protein) restored synthesis of seleno-tRNAs. In the absence of the complementary enzyme(s), the SELD protein catalyzes the synthesis of a labile selenium donor compound from selenide and ATP. 31P NMR studies show that among the products of this reaction are AMP and a compound containing selenium bonded to phosphorus. The reaction is completely dependent on the addition of both selenide and magnesium. The dependence of reaction velocity on ATP concentration shows sigmoidal kinetics, whereas dependence on selenide concentration obeys Michaelis-Menten kinetics indicating a Km value of 46 microM for selenide.

  来自沙门氏菌鼠伤寒菌的酶制剂，当添加硒化物和ATP时，催化tRNA中的5-甲基氨甲基-2-硫代尿嘧啶转化为5-甲基氨甲基-2-硒代尿嘧啶。来自携带有缺陷的selD基因的沙门氏菌突变菌株的类似制剂无法催化这种硒替代反应。然而，用纯化的selD基因产物（SELD蛋白）补充缺陷酶制剂，可以恢复硒代-tRNA的合成。在缺乏互补酶的情况下，SELD蛋白催化从硒化物和ATP中合成不稳定的硒供体化合物的反应。31P NMR研究表明，在该反应的产物中，包括AMP和含有硒与磷键合的化合物。该反应完全依赖于添加硒化物和镁。反应速率对ATP浓度的依赖呈S型动力学，而对硒化物浓度的依赖服从米氏-门特恩动力学，表明硒化物的Km值为46微米。
• Taming the Dichalcogenides: Isolation, Characterization, and Reactivity of Elusive Perselenide, Persulfide, Thioselenide, and Selenosulfide Anions
  作者：Keyan Li、Lev N. Zakharov、Michael D. Pluth

  DOI：10.1021/jacs.3c03766

  日期：2023.6.21

  Reactive sulfur species (RSS) and reactive selenium species (RSeS) play integral roles in hydrogen sulfide (H2S) and hydrogen selenide (H2Se) biological signaling pathways, and dichalcogenide anions are proposed transient intermediates that facilitate a variety of biochemical transformations. Herein we report the selective synthesis, isolation, spectroscopic and structural characterization, and fundamental

  活性硫（RSS）和活性硒（RSeS）在硫化氢（H 2 S）和硒化氢（H 2 Se）生物信号传导途径中发挥着不可或缺的作用，并且二硫属化物阴离子被认为是促进各种生化转化的瞬时中间体。在此，我们报告了过硫化物 (RSS – )、过硒化物 (RSeSe – )、硫代硒化物 (RSSe – ) 和硒硫醚 (RSeS – ) 阴离子的选择性合成、分离、光谱和结构表征以及基本反应性。分离的硫属化物不依赖于空间保护来保持稳定性，并且具有类似于半胱氨酸（Cys）的空间分布。S 8的简单还原或 Se 在 18-crown-6 存在下通过苄基硫醇钾 (KSBn) 或硒醇钾 (KSeBn) 进行反应，得到 [K(18-crown-6)][BnSS] ( 1 ), [K(18-crown- 6 ) ][BnSeSe] ( 2 )、[K(18-crown-6][BnSSe] ( 3 ) 和 [K(18-crown-6][BnSeS]
• Reaction Mechanism and Molecular Basis for Selenium/Sulfur Discrimination of Selenocysteine Lyase
  作者：Rie Omi、Suguru Kurokawa、Hisaaki Mihara、Hideyuki Hayashi、Masaru Goto、Ikuko Miyahara、Tatsuo Kurihara、Ken Hirotsu、Nobuyoshi Esaki

  DOI：10.1074/jbc.m109.084475

  日期：2010.4

  Selenocysteine lyase (SCL) catalyzes the pyridoxal 5'-phosphate-dependent removal of selenium from L-selenocysteine to yield L-alanine. The enzyme is proposed to function in the recycling of the micronutrient selenium from degraded selenoproteins containing selenocysteine residue as an essential component. The enzyme exhibits strict substrate specificity toward L-selenocysteine and no activity to its cognate L-cysteine. However, it remains unclear how the enzyme distinguishes between selenocysteine and cysteine. Here, we present mechanistic studies of selenocysteine lyase from rat. ESI-MS analysis of wild-type and C375A mutant SCL revealed that the catalytic reaction proceeds via the formation of an enzyme-bound selenopersulfide intermediate on the catalytically essential Cys-375 residue. UV-visible spectrum analysis and the crystal structure of SCL complexed with L-cysteine demonstrated that the enzyme reversibly forms a nonproductive adduct with L-cysteine. Cys-375 on the flexible loop directed L-selenocysteine, but not L-cysteine, to the correct position and orientation in the active site to initiate the catalytic reaction. These findings provide, for the first time, the basis for understanding how trace amounts of a selenium-containing substrate is distinguished from excessive amounts of its cognate sulfur-containing compound in a biological system.
• Cysteine Sulfinate Desulfinase, a NIFS-like Protein ofEscherichia coli with Selenocysteine Lyase and Cysteine Desulfurase Activities
  作者：Hisaaki Mihara、Tatsuo Kurihara、Tohru Yoshimura、Kenji Soda、Nobuyoshi Esaki

  DOI：10.1074/jbc.272.36.22417

  日期：1997.9

  Selenocysteine lyase (EC 4.4.1.16) exclusively decomposes selenocysteine to alanine and elemental selenium, whereas cysteine desulfurase (NIFS protein) of Azotobacter vinelandii acts indiscriminately on both cysteine and selenocysteine to produce elemental sulfur and selenium respectively, and alanine. These proteins exhibit some sequence homology, The Escherichia coli genome contains three genes with sequence homology to nifS. We have cloned the gene mapped at 63.4 min in the chromosome and have expressed, purified to homogeneity, and characterized the gene product, The enzyme comprises two identical subunits with 401 amino acid residues (M-r 43,238) and contains pyridoxal 5'-phosphate as a coenzyme. The enzyme catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine, Because L-cysteine sulfinic acid was desulfinated to form L-alanine as the preferred substrate, we have named this new enzyme cysteine sulfinate desulfinase. Mutant enzymes having alanine substituted for each of the four cysteinyl residues (Cys-100, Cys-176, Cys-323, and Cys-358) were all active, Cys-358 corresponds to Cys-325 of A. vinelandii NIFS, which is conserved among all NIFS-like proteins and catalytically essential (Zheng, L., White, R. H., Cash, V. L., and Dean, D. R. (1994) Biochemistry 33, 4714-4720), is not required for cysteine sulfinate desulfinase. Thus, the enzyme is distinct from A. vinelandii NIFS in this respect.