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Zinc Thiolate Complexes of (N,N,S)‐Tridentate Ligands for the Modeling of Thiolate Alkylating Enzymes
Author(s) -
Ji Mian,
Vahrenkamp Heinrich
Publication year - 2005
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.200400927
Subject(s) - chemistry , zinc , methylamine , ligand (biochemistry) , medicinal chemistry , coordination sphere , amine gas treating , pyridine , iodide , stereochemistry , deprotonation , crystal structure , ion , organic chemistry , biochemistry , receptor
Zinc thiolate complexes of three tridentate (N,N,S) ligands were prepared as models for the structure and function of thiolate alkylating zinc enzymes. N ‐(2‐Mercaptoisobutyl)(2‐pyridin‐2‐yl‐methyl)amine ( L 1 ) forms isobutylthiolate‐bridged dinuclear complexes with ZnN 2 S 3 coordination. N ‐(2‐Mercaptoisobutyl)(2‐pyridin‐2‐yl‐ethyl)amine ( L 2 ) yields isobutylthiolate‐bridged dinuclear complexes in which the pyridine donor is not coordinated to zinc, resulting in a ZnNS 3 coordination. Only N ‐(2‐mercaptoisobutyl)(2‐pyridin‐2‐yl‐ethyl)methylamine ( L 3 ) forms the desired mononuclear complexes with ZnN 2 S 2 coordination. The latter react with the alkylating agents CH 3 I and PO(OCH 3 ) 3 in a two‐step process. In the first step the isobutylthiolate function is methylated and its position in the ligand sphere of zinc is taken by I – or OPO(OCH 3 ) 2 – , respectively, and in the second step the additional thiolate ligand is methylated and replaced by a second iodide or dimethyl phosphate anion. (© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2005)