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Zinc Thiolate Complexes [ZnL n (SR)] + with Azamacrocyclic Ligands: Synthesis and Structural Properties
Author(s) -
Notni Johannes,
Görls Helmar,
Anders Ernst
Publication year - 2006
Publication title -
european journal of inorganic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.667
H-Index - 136
eISSN - 1099-0682
pISSN - 1434-1948
DOI - 10.1002/ejic.200500947
Subject(s) - chemistry , zinc , ligand (biochemistry) , stereochemistry , tetracoordinate , monomer , crystallography , molecule , crystal structure , polymer , organic chemistry , receptor , biochemistry , computer graphics (images) , computer science , planar
A series of 24 novel zinc thiolate complexes containing saturated macrocyclic polyamine ligands with the general formula [Zn(L n )(SR)]ClO 4 (L n : n ‐dentate azamacrocyclic ligand) has been synthesized. Two different thiolate ligands (R = phenyl, benzyl) and 12 macrocyclic ligands with ring sizes varying from 11 to 16 atoms and containing three, four, and five nitrogen donors (including a new macrocyclic triamine ligand, 8‐methyl‐[11]aneN 3 ) have been used. The solid‐state structures of 20 of the 24 complexes have been characterized by X‐ray diffraction. The crystal lattice of all compounds is comprised exclusively of monomers. The tetracoordinate N 3 S compounds exhibit Zn–S bond lengths ranging from 2.2259(5) to 2.2492(9) Å and the pentacoordinate N 4 S systems from 2.266(2) to 2.3200(7) Å. In addition, two complexes with the very rare N 5 S coordination environment for zinc have been found. They exhibit Zn–S bond lengths of 2.3782(7) and 2.42 Å (mean value of two independent molecules). The thiolate complexes are suitable model systems for the precursor proteins of matrix metalloproteases (pro‐MMPs) as well as for thiolate alkylating enzymes such as cobalamine‐dependent/independent methionine synthases, farnesyl transferase, and the Ada repair protein. (© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2006)