A structural and catalytic model for zinc phosphoesterases

Rebecca R. Buchholz, Morgan E. Etienne, Anneke Dorgelo, Ruth E. Mirams, Sarah J. Smith, Shiao Yun Chow, Lyall R. Hanton, Geoffrey B. Jameson, Gerhard Schenk, Lawrence R. Gahan

Research output: Contribution to journalArticlepeer-review

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 [Zn 2(HL1)(CH3COO)](PF6)·H2O and Li[Zn2(HL1)]4(PO4)2(PF 6)3·(CH3OH). The ligand (H 3L1) and complex [Zn2(HL1)(CH3COO)](PF 6)·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.

Original languageEnglish
Pages (from-to)6045-6054
Number of pages10
JournalDalton Transactions
Issue number43
DOIs
Publication statusPublished - 6 Nov 2008

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