Neves, Ademir and Lanznaster, Mauricio and Bortoluzzi, Adailton J. and Peralta, Rosely A. and Casellato, Annelise and Castellano, Eduardo Ernesto and Herrald, Paul and Riley, Mark J. and Schenk, Gerhard (2007) An Unprecedented FeIII(μ-OH)ZnII Complex that Mimics the Structural and Functional Properties of Purple Acid Phosphatases. Journal of the American Chemical Society, 129 (24). pp. 7486-7487. ISSN 0002-7863

Download (62kB)

Abstract

This communication reports the synthesis and X-ray structure of the first mixed-valence FeIIIZnII complex containing the FeIII(μ-OH)ZnII structural unit. Based on the structure, physicochemical solution studies, and the catalytic properties toward the hydrolysis of the diester 2,4-bis(dinitrophenyl)phosphate (BDNPP), it is proposed that complex 1 employs a hydrolytic mechanism similar to that proposed for red kidney bean purple acid phosphatase, including a nucleophilic attack by the terminal, FeIII-bound hydroxide and the concomitant release of 2,4-dinitrophenolate. Furthermore, it is demonstrated that the μ-hydroxo group in the {FeIII(μ-OH)(μ-ROPO3)ZnII} intermediate is unable to hydrolyze the monoester 2,4-dinitrophenylphosphate (DNPP), which suggests that the μ-hydroxo group is a significantly poorer nucleophile than the terminally FeIII-bound OH- group.

Item Type:	Article
Additional Information:	The definitive version of this article is available in the Journal of the American Chemical Society, 2007, 129 (24), pp 7486–7487, DOI: 10.1021/ja071184l. Copyright © 2007 American Chemical Society
Keywords:	FeIII(μ-OH)ZnII; Complex; Structural; Functional; Properties; Purple Acid Phosphatases;
Academic Unit:	Faculty of Science and Engineering > Chemistry
Item ID:	3702
Depositing User:	Gary Schenk
Date Deposited:	29 May 2012 15:29
Journal or Publication Title:	Journal of the American Chemical Society
Publisher:	American Chemical Society
Refereed:	Yes
URI:	http://portal.acs.org/portal/acs/corg/co...
Use Licence:	This item is available under a Creative Commons Attribution Non Commercial Share Alike Licence (CC BY-NC-SA). Details of this licence are available here

Repository Staff Only(login required)

Item control page

Downloads

Origin of downloads