Química Nova (Apr 1997)

Modelando a coordenação de fosfato com o sítio ativo das fosfatases ácidas púrpuras Modeling the coordination of phosphate to the active site of purple acid phosphatases

  • Marcos Aires de Brito,
  • Ademir Neves,
  • Luiz R. Zilli

DOI
https://doi.org/10.1590/S0100-40421997000200007
Journal volume & issue
Vol. 20, no. 2
pp. 154 – 157

Abstract

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We present a new binuclear complex, Fe2III(BBPMP)(OH)(O2 P(OPh)2) ClO4.CH3OH, 3, where BBPMP is the anion of 2,6-bis(2-hydroxybenzyl)(2-pyridylmethyl) aminomethyl-4-methylphenol, as a suitable model for the chromophoric site of purple acid phosphatases coordinated to phosphate. The complex was obtained by the reaction of complex 2, Fe2III(BBPMP)(O2P(OPh) 2)2 ClO4.H2O, in CH3CN with one equivalent of triethylamine. Based on the chromophoric properties of the model complex, lmax = 560 nm/ e = 4480 M-1 cm-1/Fe2 compared to the enzyme coordinated to phosphate, we can speculate about a possible mechanism of fixing this oxyanion by the oxidized form of the enzymes.

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