cis-Pd(1,5-dithiacyclooctan-3-ol)Cl2 | 218448-97-6

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: cis-Pd(1,5-dithiacyclooctan-3-ol)Cl2
• CAS: 218448-97-6
• 化学式: C₆H₁₂Cl₂OPdS₂
• 分子量: 341.619
• InChiKey: GDXYLLGYYPBWOF-UHFFFAOYSA-L

计算性质

• 辛醇/水分配系数(LogP)：
  None
• 重原子数：
  None
• 可旋转键数：
  None
• 环数：
  None
• sp3杂化的碳原子比例：
  None
• 拓扑面积：
  None
• 氢给体数：
  None
• 氢受体数：
  None

反应信息

• 作为反应物：
  描述：

  cis-Pd(1,5-dithiacyclooctan-3-ol)Cl2 、 水 在 AgCF₃SO₃ 作用下， 以 not given 为溶剂， 生成 [cis-Pd(1,5-dithiacyclooctan-3-ol)(water)2](2+)
  参考文献：
  名称：

  Sequence-dependent cleavage of albumins with palladium(II) complexes: role of serine residue in controlling the high regioselectivity of protein cleavage

  摘要：

  Bovine serum, pig serum, and chicken egg albumins were incubated at 60 degreesC for 2 days or at 50 degreesC for 6 days with the pyridine (py) complex trans-[Pd(py)(2)(H2O)(2)](2+), the ethylenediamine (en) complex cis-[Pd(en)(H2O)(2)](2+), the 1,4-diazacycloheptane (dach) complex cis-[Pd(dach)(H2O)(2)](2+), and the 1,5-dithiacyclooctan-3-ol (dtco-3-OH) complex cis-[Pd(dtco-3-OH)(H2O)(2)](2+) at pH 4.5 +/- 0.2. The mole ratio of the complex and the protein was 8:1 or 16:1. Except for cis-[Pd(dtco-3-OH)(H2O)(2)](2+), which was unreactive, the remaining three palladium(H) complexes consistently cleaved bovine albumin at the sites Glu57-Ser58, Gly85-Asp86, Leu103-Ser104, and Lys285-Ser286; pig albumin at the site Lys285-Ser286; and chicken albumin at the sites Ala6-Ser7, Ala220-Ser221, Gly237-Thr238, and Met239-Ser240. With all the three active Pd(II) complexes and all the three proteins, each site of major cleavage is a peptide bond followed by two residues, the first of which is serine or threonine and the second of which is histidine or methionine. The latter of the two residues serves as an anchor for the Pd(H) complex, The former of the two residues, with its alcoholic side chain, seems to guide the cleavage of the peptide bond immediately preceding it. To explain this guidance, we optimized the geometry of the relevant tripeptide complex [Pd(OH)(Ac-Gly-SerH(-1)-MetH(-1)-NMe-kappa(3)N(S),N-M,S](-) by MM+ and ZINDO/1 calculations. A mechanism involving the nucleophilic attack of the hydroxylic group of serine on the carbonyl carbon atom of glycine resembles the catalytic mechanism of serine proteases. (C) 2002 Elsevier Science B.V. All rights reserved.

  DOI：

  10.1016/s0020-1693(02)00928-3

文献信息

• Kaminskaia, Natalia V.; Kostic, Nenad M., Journal of the Chemical Society, Dalton Transactions, 1996, # 18, p. 3677 - 3686
  作者：Kaminskaia, Natalia V.、Kostic, Nenad M.

  DOI：——

  日期：——
• Sequence-dependent cleavage of albumins with palladium(II) complexes: role of serine residue in controlling the high regioselectivity of protein cleavage
  作者：Longgen Zhu、Nenad M. Kostić

  DOI：10.1016/s0020-1693(02)00928-3

  日期：2002.11

  Bovine serum, pig serum, and chicken egg albumins were incubated at 60 degreesC for 2 days or at 50 degreesC for 6 days with the pyridine (py) complex trans-[Pd(py)(2)(H2O)(2)](2+), the ethylenediamine (en) complex cis-[Pd(en)(H2O)(2)](2+), the 1,4-diazacycloheptane (dach) complex cis-[Pd(dach)(H2O)(2)](2+), and the 1,5-dithiacyclooctan-3-ol (dtco-3-OH) complex cis-[Pd(dtco-3-OH)(H2O)(2)](2+) at pH 4.5 +/- 0.2. The mole ratio of the complex and the protein was 8:1 or 16:1. Except for cis-[Pd(dtco-3-OH)(H2O)(2)](2+), which was unreactive, the remaining three palladium(H) complexes consistently cleaved bovine albumin at the sites Glu57-Ser58, Gly85-Asp86, Leu103-Ser104, and Lys285-Ser286; pig albumin at the site Lys285-Ser286; and chicken albumin at the sites Ala6-Ser7, Ala220-Ser221, Gly237-Thr238, and Met239-Ser240. With all the three active Pd(II) complexes and all the three proteins, each site of major cleavage is a peptide bond followed by two residues, the first of which is serine or threonine and the second of which is histidine or methionine. The latter of the two residues serves as an anchor for the Pd(H) complex, The former of the two residues, with its alcoholic side chain, seems to guide the cleavage of the peptide bond immediately preceding it. To explain this guidance, we optimized the geometry of the relevant tripeptide complex [Pd(OH)(Ac-Gly-SerH(-1)-MetH(-1)-NMe-kappa(3)N(S),N-M,S](-) by MM+ and ZINDO/1 calculations. A mechanism involving the nucleophilic attack of the hydroxylic group of serine on the carbonyl carbon atom of glycine resembles the catalytic mechanism of serine proteases. (C) 2002 Elsevier Science B.V. All rights reserved.