FeIIIFeIII and FeIIFeIII Complexes as Synthetic Analogues for the Oxidized and Reduced Forms of Purple Acid Phosphatases
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- 作者：Ademir Neves and ; Marcos A. de Brito ; Ivo Vencato ; Valderes Drago ; Klaus Griesar ; and Wolfgang Haase
- 刊名：Inorganic Chemistry
- 出版年：1996
- 出版时间：April 10, 1996
- 年：1996
- 卷：35
- 期：8
- 页码：2360 - 2368
- 全文大小：355K
- 年卷期：v.35,no.8(April 10, 1996)
- ISSN：1520-510X
文摘
Novel FeIIIFeIII andFeIIFeIII complexes[Fe2(BBPMP)(
-OAc)(-X)]n(1, X = OAc-, n = 1+;2, X = OH-, n =1+; 3, X = OAc-, n = 0;4, X = OH-, n = 0), whereBBPMP3- is the anion of2,6-bis[(2-hydroxybenzyl)(2-pyridylmethyl)aminomethyl]-4-methylphenol, and OAc-is acetate, were prepared in order to provide models forthe active site of purple acid phosphatases (PAPs). Complex1 was obtained by the reaction of H3BBPMPwithFe(ClO4)2·6H2O inmethanol and sodium acetate trihydrate under ambient conditions, whilecomplex 3 wassynthesized as described for 1, under an argon atmospherewith low levels of dioxygen. 2 was isolated from1in acetonitrile by a substitution of the bridging acetate group byhydroxide, while 4 was generated in solutionduring a spectropotentiostatic experiment on 2, under argon.Complex 1,[FeIII2(BBPMP)(-OAc)2]ClO4·H2O,has been characterized by X-ray crystallography. Crystal data:monoclinic, space group P21/n,a = 14.863(5) Å,b = 12.315(3) Å, c = 20.872(8) Å,
= 90.83(3)
, Z = 4. IR, Mössbauer,magnetic, electronic absorption, andelectrochemical properties of 1-3 have beeninvestigated, and some of these properties represent acontributionto the understanding of the dinuclear iron center of PAPs.Complexes 2,[FeIII2(BBPMP)(-OAc)(-OH)]ClO4(
max = 568 nm/
= 4760M-1 cm-1), and4[FeIIFeIII(BBPMP)(-OAc)(-OH)](max = 516 nm/ = 4560M-1cm-1), constitute good synthetic analoguesfor the chromophoric site for the oxidized and reducedforms,respectively, of the enzyme.
-OAc)(-X)]n(1, X = OAc-, n = 1+;2, X = OH-, n =1+; 3, X = OAc-, n = 0;4, X = OH-, n = 0), whereBBPMP3- is the anion of2,6-bis[(2-hydroxybenzyl)(2-pyridylmethyl)aminomethyl]-4-methylphenol, and OAc-is acetate, were prepared in order to provide models forthe active site of purple acid phosphatases (PAPs). Complex1 was obtained by the reaction of H3BBPMPwithFe(ClO4)2·6H2O inmethanol and sodium acetate trihydrate under ambient conditions, whilecomplex 3 wassynthesized as described for 1, under an argon atmospherewith low levels of dioxygen. 2 was isolated from1in acetonitrile by a substitution of the bridging acetate group byhydroxide, while 4 was generated in solutionduring a spectropotentiostatic experiment on 2, under argon.Complex 1,[FeIII2(BBPMP)(-OAc)2]ClO4·H2O,has been characterized by X-ray crystallography. Crystal data:monoclinic, space group P21/n,a = 14.863(5) Å,b = 12.315(3) Å, c = 20.872(8) Å, = 90.83(3), Z = 4. IR, Mössbauer,magnetic, electronic absorption, andelectrochemical properties of 1-3 have beeninvestigated, and some of these properties represent acontributionto the understanding of the dinuclear iron center of PAPs.Complexes 2,[FeIII2(BBPMP)(-OAc)(-OH)]ClO4(max = 568 nm/ = 4760M-1 cm-1), and4[FeIIFeIII(BBPMP)(-OAc)(-OH)](max = 516 nm/ = 4560M-1cm-1), constitute good synthetic analoguesfor the chromophoric site for the oxidized and reducedforms,respectively, of the enzyme.