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Dinuclear Zinc(II)−Iron(III) and Iron(II)−Iron(III) Complexes as Models for Purple Acid Phosphatases
Author(s) -
Albedyhl Sabine,
AverbuchPouchot Marie Therese,
Belle Catherine,
Krebs Bernt,
Pierre Jean Louis,
SaintAman Eric,
Torelli Stephane
Publication year - 2001
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 - 10.1002/1099-0682(200106)2001:6<1457::aid-ejic1457>3.0.co;2-f
Subject(s) - chemistry , zinc , phosphodiester bond , isostructural , ligand (biochemistry) , acetonitrile , stereochemistry , catalysis , medicinal chemistry , metal , coordination sphere , inorganic chemistry , crystal structure , crystallography , organic chemistry , receptor , biochemistry , rna , gene
Abstract The heterodinuclear Zn II Fe III complex 1 and the isostructural Fe II Fe III complex 2 with the dinucleating ligand from 2,6‐bis[{bis(2‐pyridylmethyl)amino}methyl]‐4‐methoxyphenol (HBPMOP, 3 ) were prepared and characterized by X‐ray crystallography. Solution studies (UV/Vis spectroscopy; electrochemistry) are described. A pH‐induced change in the coordination spheres of the metal centers is seen. These complexes serve as models for the mixed‐valence oxidation state in purple acid phosphatases. The cleavage acceleration of the activated phosphodiester 2‐hydroxypropyl p ‐nitrophenyl phosphate (HPNP) was investigated in acetonitrile/water (1:1) in the presence of complexes of the ligand BPMOP and its methyl analogue BPMP with regards to its dependence on the pH value. At the optimum pH value (8.5 ± 0.2), the Zn II Fe III complex from BPMOP shows a 2‐fold higher rate acceleration compared with that of the complex containing BPMP. The diiron complex from BPMOP is 4‐fold more reactive than the homologous complex from BPMP. The heterodinuclear Zn II Fe III catalysts are at least 10‐fold more reactive than the homonuclear Fe II Fe III catalysts.