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Structural and Functional Models of the Active Site of Zinc Phosphotriesterase

Carlsson, Håkan LU orcid ; Haukka, Matti and Nordlander, Ebbe LU (2004) In Inorganic Chemistry 43(18). p.5681-5687
Abstract
In an attempt to prepare structural and functional models for the active site of the hydrolytic enzyme zinc phosphotriesterase, five new zinc complexes of the ligands 2,6-bis[N-(N-(carboxylmethyl)-N-((1-methylimidazol)methyl)amine)methyl]-4-methylphenolate (BCIMP) and the corresponding asymmetric ligand 2-(N-isopropyl-N-((1-methylimidazolyl)methyl)aminomethyl)-6-(N-carboxylmethyl-N-((1-methylimidazolyl)methyl)aminomethyl)-4-methylphenol (ICIMP) have been synthesized, viz. Na[Zn2(BCIMP)Ac2] (1), [Zn2(BCIMP)(Ph2Ac)] (2), [Zn2(ICIMP)Ac2] (3), [Zn4(ICIMP)2(Me3Ac)2][ClO4]2 (4), and [Zn4(ICIMP)2(Ph2Ac)2][ClO4]2 (5). The X-ray structure of complex 5 has been determined and reveals that the complex is a dimer of dimers in the solid state, which in... (More)
In an attempt to prepare structural and functional models for the active site of the hydrolytic enzyme zinc phosphotriesterase, five new zinc complexes of the ligands 2,6-bis[N-(N-(carboxylmethyl)-N-((1-methylimidazol)methyl)amine)methyl]-4-methylphenolate (BCIMP) and the corresponding asymmetric ligand 2-(N-isopropyl-N-((1-methylimidazolyl)methyl)aminomethyl)-6-(N-carboxylmethyl-N-((1-methylimidazolyl)methyl)aminomethyl)-4-methylphenol (ICIMP) have been synthesized, viz. Na[Zn2(BCIMP)Ac2] (1), [Zn2(BCIMP)(Ph2Ac)] (2), [Zn2(ICIMP)Ac2] (3), [Zn4(ICIMP)2(Me3Ac)2][ClO4]2 (4), and [Zn4(ICIMP)2(Ph2Ac)2][ClO4]2 (5). The X-ray structure of complex 5 has been determined and reveals that the complex is a dimer of dimers in the solid state, which in solution dissociates to potent structural models. Studies using NMR show that only one carboxylate coligand bridges the dizinc units in the case of diphenyl acetate and pivalate, while the steric bulk of acetate is sufficiently small to permit the coordination of two acetates/dizinc unit. Functional studies involving the hydrolysis/transesterification of 2-hydroxypropyl p-nitrophenyl phosphate (HPNP) show that the complex with ICIMP (compound 5) has a significantly higher rate of catalysis than the BCIMP complex (compound 2). This is attributed to the vacant/labile coordination site that is available in the ICIMP complex but not the BCIMP complex. (Less)
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author
; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Inorganic Chemistry
volume
43
issue
18
pages
5681 - 5687
publisher
The American Chemical Society (ACS)
external identifiers
  • pmid:15332820
  • wos:000223680200028
  • scopus:4444358989
  • pmid:15332820
ISSN
1520-510X
DOI
10.1021/ic0354522
language
English
LU publication?
yes
id
18235750-c92e-4541-a9e0-2be2780410f0 (old id 141543)
date added to LUP
2016-04-01 11:53:49
date last changed
2022-01-26 19:53:48
@article{18235750-c92e-4541-a9e0-2be2780410f0,
  abstract     = {{In an attempt to prepare structural and functional models for the active site of the hydrolytic enzyme zinc phosphotriesterase, five new zinc complexes of the ligands 2,6-bis[N-(N-(carboxylmethyl)-N-((1-methylimidazol)methyl)amine)methyl]-4-methylphenolate (BCIMP) and the corresponding asymmetric ligand 2-(N-isopropyl-N-((1-methylimidazolyl)methyl)aminomethyl)-6-(N-carboxylmethyl-N-((1-methylimidazolyl)methyl)aminomethyl)-4-methylphenol (ICIMP) have been synthesized, viz. Na[Zn2(BCIMP)Ac2] (1), [Zn2(BCIMP)(Ph2Ac)] (2), [Zn2(ICIMP)Ac2] (3), [Zn4(ICIMP)2(Me3Ac)2][ClO4]2 (4), and [Zn4(ICIMP)2(Ph2Ac)2][ClO4]2 (5). The X-ray structure of complex 5 has been determined and reveals that the complex is a dimer of dimers in the solid state, which in solution dissociates to potent structural models. Studies using NMR show that only one carboxylate coligand bridges the dizinc units in the case of diphenyl acetate and pivalate, while the steric bulk of acetate is sufficiently small to permit the coordination of two acetates/dizinc unit. Functional studies involving the hydrolysis/transesterification of 2-hydroxypropyl p-nitrophenyl phosphate (HPNP) show that the complex with ICIMP (compound 5) has a significantly higher rate of catalysis than the BCIMP complex (compound 2). This is attributed to the vacant/labile coordination site that is available in the ICIMP complex but not the BCIMP complex.}},
  author       = {{Carlsson, Håkan and Haukka, Matti and Nordlander, Ebbe}},
  issn         = {{1520-510X}},
  language     = {{eng}},
  number       = {{18}},
  pages        = {{5681--5687}},
  publisher    = {{The American Chemical Society (ACS)}},
  series       = {{Inorganic Chemistry}},
  title        = {{Structural and Functional Models of the Active Site of Zinc Phosphotriesterase}},
  url          = {{http://dx.doi.org/10.1021/ic0354522}},
  doi          = {{10.1021/ic0354522}},
  volume       = {{43}},
  year         = {{2004}},
}