Plasticity in the copper-thioether bond: manifestation in blue Cu proteins and in synthetic analogs.
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).
Leiden Institute of Chemistry, Leiden University, P.O. Box 9502, 2300 RA, Leiden, The Netherlands.
Jan
J
Reedijk
D040761:Biomimetic Materials / Q000737:chemistry*; D003300:Copper / Q000737:chemistry*; D008667:Metalloproteins / Q000737:chemistry; D008715:Methionine / Q000737:chemistry*; D013440:Sulfides / Q000737:chemistry*
D008667:Metalloproteins; D013440:Sulfides; D003300:Copper; D008715:Methionine