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A Novel Water‐Soluble Tripodal Imidazolyl Ligand as a Model for the Tris(histidine) Motif of Zinc Enzymes: Nickel, Cobalt and Zinc Complexes and a Comparison with Metal Binding in Carbonic Anhydrase
Author(s) -
Kunz Peter C.,
Reiß Guido J.,
Frank Walter,
Kläui Wolfgang
Publication year - 2003
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.200300228
Subject(s) - chemistry , carbonic anhydrase , zinc , tris , cobalt , nickel , ligand (biochemistry) , histidine , carbonic anhydrase ii , metal , methanol , medicinal chemistry , stereochemistry , aqueous solution , tripodal ligand , crystal structure , inorganic chemistry , enzyme , polymer chemistry , organic chemistry , receptor , biochemistry
Tris[2‐isopropylimidazol‐4(5)‐yl]phosphane (4‐TIP i Pr ), a novel model ligand for the tris(histidine) motif of many zinc enzymes, has been prepared. 4‐TIP i Pr is hydrolytically stable and soluble in protic solvents. It readily forms chloro‐ and nitratocobalt, ‐nickel and ‐zinc complexes in aqueous methanol. The crystal structures of the solvates [(4‐TIP i Pr )Co(MeOH)(NO 3 )]NO 3 ·2Et 2 O ( 3· 2Et 2 O), [(4‐TIP i Pr )Ni(MeOH)(NO 3 )]NO 3 ·Et 2 O·MeOH ( 4· Et 2 O·MeOH), [(4‐TIP i Pr )CoCl]Cl·MeOH·2.5H 2 O ( 5· MeOH·2.5H 2 O), and [(4‐TIP i Pr )ZnCl]Cl·MeOH·2.5H 2 O ( 6· MeOH·2.5H 2 O) have been determined. The complex 3 shows striking structural similarities to the hydrogencarbonate complex of cobalt‐substituted human carbonic anhydrase II (HCA II). (© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2003)