[(tris(2-aminoethyl)amine)Zn(bis(4-nitrophenyl)phosphato)](ClO4) | 339063-42-2

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: [(tris(2-aminoethyl)amine)Zn(bis(4-nitrophenyl)phosphato)](ClO4)
• CAS: 339063-42-2
• 化学式: C₁₈H₂₆N₆O₈PZn*ClO₄
• 分子量: 650.254
• InChiKey: CVAWIBFLLNGGLK-UHFFFAOYSA-L

计算性质

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

• 作为产物：
  描述：

  [(tris(2-aminoethyl)amine)Zn(OH2)](ClO4)2 、 双(对硝基苯基)磷酸酯 以 水 为溶剂， 生成 [(tris(2-aminoethyl)amine)Zn(bis(4-nitrophenyl)phosphato)](ClO4)
  参考文献：
  名称：

  Phosphoester hydrolysis using structural phosphatase models of tren based zinc(II) complexes and X-ray crystal structures of [Zn(tren)(H2O)](ClO4)2 and [Zn(tren)(BNPP)]ClO4

  摘要：

  New tris(2-aminoethyl)amine (tren) L1 based ligands, namely N,N',N"-tris(2-benzylaminoethyl)amine L2 and N,N',N"-tris(imbenzyl-L-histidylethylaminoethyl) amine L3 have been synthesized and characterized. Complexation studies on Zn2+ complexes 1, 2 and 3 derived from L1, L2, and L3 showed that the presence of benzyl and benzyl-histidyl moieties attached to the tripodal ligand L1 side arms decrease the pK(a) of the Zn-bound water molecule: 10.72 for 1, 9.61 for 2 and 7.43 for 3, respectively. The zinc complex of 3 was a much more active catalyst for the hydrolysis of bis(p-nitrophenyl)phosphate (BNPP-) and tris(p-nitrophenyl)phosphate (TNPP)compared with 1 and 2. In the case of 1 and 2, the pH-dependence of their observed pseudo-first-order rate constants k(obsd) showed sigmoidal pH-rate profile, while 3 gave bell-shape curve with a maximum rate constant of around 1.0 x 10 (5) s(-1) at pN 8.5. The pH dependence of k(obsd) indicated that the Zn-bound hydroxo species is responsible for catalytic activity. The crystal structures of [L1Zn-H2O](2+) (1) and [L1Zn-BNPP](+) (4) have been determined and showed trigonal-bipyramidal configurations around the central Zn. The zinc complexes of 1 and 4 served as structural models for the binding mode of coordinated water as well as substrates in the active site of zinc enzyme. (C) 2001 Elsevier Science B.V. All rights reserved.

  DOI：

  10.1016/s0020-1693(00)00381-9