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Issue 43, 2008
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A structural and catalytic model for zinc phosphoesterases

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Abstract

A structural model for the active site of phosphoesterases, enzymes that degrade organophosphate neurotoxins, has been synthesised. The ligand [2-((2-hydroxy-3-(((2-hydroxyethyl)(pyridin-2-ylmethyl)amino)methyl)-5-methylbenzyl)(pyridin-2-ylmethyl)amino)acetic acid] (H3L1) and two Zn(II) complexes have been prepared and characterised as [Zn2(HL1)(CH3COO)](PF6)·H2O and Li[Zn2(HL1)]4(PO4)2(PF6)3·(CH3OH). The ligand (H3L1) and complex [Zn2(HL1)(CH3COO)](PF6)·H2O were characterised through 1H NMR, 13C NMR, mass spectroscopy and microanalysis. The X-ray crystal structure of Li[Zn2(HL1)]4(PO4)2(PF6)3·(CH3OH) revealed a tetramer of dinuclear complexes, bridged by two phosphate molecules and bifurcating acetic acid arms. Functional studies of the zinc complex with the substrate bis(4-nitrophenyl)phosphate (bNPP) determined the complex with HL12− to be a competent catalyst with kcat = 1.26 ± 0.06 × 10−6 s−1.

Graphical abstract: A structural and catalytic model for zinc phosphoesterases

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Publication details

The article was received on 24 Apr 2008, accepted on 04 Aug 2008 and first published on 23 Sep 2008


Article type: Paper
DOI: 10.1039/B806391E
Citation: Dalton Trans., 2008,0, 6045-6054
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    A structural and catalytic model for zinc phosphoesterases

    R. R. Buchholz, M. E. Etienne, A. Dorgelo, R. E. Mirams, S. J. Smith, S. Y. Chow, L. R. Hanton, G. B. Jameson, G. Schenk and L. R. Gahan, Dalton Trans., 2008, 0, 6045
    DOI: 10.1039/B806391E

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