García-Tojal J, García-Orad A, Serra J L, Pizarro J L, Lezama L, Arriortua M I, Rojo T
Departamento de Química, Universidad de Burgos, Spain.
J Inorg Biochem. 1999 May 30;75(1):45-54. doi: 10.1016/S0162-0134(99)00031-8.
The synthesis, structure and spectroscopic properties on complexes with the formula [Cu(Lm)2] (1) and Cu(NO3)2(HLm)2 (2), where HLm = thiophene-2-carbaldehyde thiosemicarbazone, have been developed. The molecular structure of compound 1 consists of monomeric entities. The copper(II) ions exhibit distorted square-planar geometry with both bidentate thiosemicarbazone ligands placed in a centrosymmetric way. Metal to ligand pi-backdonation is proposed to explain several structural and spectroscopic features in these complexes. The EPR spectra of compound 1 show an orthorhombic g tensor indicating the presence of weak magnetic exchange interactions. The reaction of compound 1 with glutathione causes the reduction of the metal ion and the substitution of the thiosemicarbazone ligand by the thiol ligand. This mechanism seems to be related to the cytotoxicity of this complex against Friend Erithroleukemia cells (FLC) and melanome B16F10 cells.
已对化学式为[Cu(Lm)₂] (1) 和Cu(NO₃)₂(HLm)₂ (2) 的配合物的合成、结构及光谱性质展开研究,其中HLm = 噻吩-2-甲醛缩氨基硫脲。化合物1的分子结构由单体实体组成。铜(II) 离子呈现扭曲的平面正方形几何构型,两个双齿缩氨基硫脲配体呈中心对称排列。有人提出金属到配体的π-反馈键来解释这些配合物中的几个结构和光谱特征。化合物1的电子顺磁共振光谱显示出正交的g张量,表明存在弱磁交换相互作用。化合物1与谷胱甘肽的反应导致金属离子还原以及缩氨基硫脲配体被硫醇配体取代。这种机制似乎与该配合物对弗氏红白血病细胞 (FLC) 和黑色素瘤B16F10细胞的细胞毒性有关。