Plasticity in the copper-thioether bond: Manifestation in blue Cu proteins and in synthetic analogs

被引:13
作者
Reedijk, Jan [1 ,2 ]
机构
[1] Leiden Univ, Leiden Inst Chem, NL-2300 RA Leiden, Netherlands
[2] King Saud Univ, Dept Chem, Riyadh 11451, Saudi Arabia
关键词
Copper; Thioether; Biomimetic; Plasticity; Zinc; X-RAY-STRUCTURE; METAL-ION COMPLEXES; CRYSTAL-STRUCTURE; COORDINATION-COMPOUNDS; MOLECULAR-STRUCTURE; TRANSPORTER CTR1; DONOR LIGANDS; ZINC TRIAD; I COPPER; SPECTROSCOPIC PROPERTIES;
D O I
10.1016/j.jinorgbio.2012.01.006
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 angstrom, 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). (C) 2012 Elsevier Inc. All rights reserved.
引用
收藏
页码:182 / 185
页数:4
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