Leiden Institute of Chemistry, Leiden University, P.O. Box 9502, 2300 RA, Leiden, The Netherlands.
J Inorg Biochem. 2012 Oct;115:182-5. doi: 10.1016/j.jinorgbio.2012.01.006. Epub 2012 Jan 23.
The binding of thioethers to transition metals in biological and biomimetic systems is reviewed with a focus on copper. Literature data show that copper(I) ions have a stronger tendency to bind thioethers, e.g. methionine-like ligands, than the isoelectronic Zn(II) ions. The plasticity in the Cu(II) coordination sphere, and the diffuseness of the lone pair electrons of a thioether sulfur, allow Cu(II)-S(thioether) bond distances to vary from 2.4 to 3.2 Å, as shown by an in-depth analysis of protein structures (Protein Structure Database, PDB) and molecular structures of copper coordination compounds (Cambridge Structural Database, CSD).
本文综述了生物和仿生体系中硫醚与过渡金属的结合，重点关注铜。文献数据表明，与等电子的 Zn(II) 离子相比，铜 (I) 离子更容易与硫醚（如蛋氨酸样配体）结合。铜 (II) 配合物的配位空间具有较强的可变性，硫醚硫原子的孤对电子较为弥散，因此，蛋白结构（蛋白质结构数据库，PDB）和铜配合物的分子结构（剑桥结构数据库，CSD）的深入分析表明，Cu(II)-S(硫醚)键的距离可在 2.4 至 3.2 Å 之间变化。
