STRUCTURE OF A MONONUCLEAR IRON(II)-CATECHOLATE COMPLEX AND ITS RELEVANCE TO THE EXTRADIOL-CLEAVING CATECHOL DIOXYGENASES

被引：53

作者：

CHIOU, YM ^{[1
]}

QUE, L ^{[1
]}

机构：

[1] UNIV MINNESOTA,DEPT CHEM,MINNEAPOLIS,MN 55455

来源：

INORGANIC CHEMISTRY | 1995年 / 34卷 / 14期

关键词：

D O I：

10.1021/ic00118a001

中图分类号：

O61 [无机化学];

学科分类号：

070301 ; 081704 ;

摘要：

The first mononuclear iron(II)-catecholate complex, [Fe-II(6TLA)(DBCH)](ClO4) (1), has been synthesized as a model for the enzyme-substrate complex of extradiol-cleaving catechol dioxygenases. Complex 1 features a bidentate but monoanionic DBCH ligand, which gives rise to significantly different Fe-O(catecholate) bond lengths. The short Fe-O bond in 1 nearly matches the 1.93 Angstrom Fe-O distance found for the enzyme-substrate complex of catechol 2,3-dioxygenase, making 1 a plausible structural model for this enzyme complex.

引用

页码：3577 / 3578

页数：2

共 23 条

[1]

ARCIERO DM, 1983, J BIOL CHEM, V258, P4981

[2]

ARCIERO DM, 1985, J BIOL CHEM, V260, P4035

[3]

ARCIERO DM, 1986, J BIOL CHEM, V261, P2170

[4] MODELS FOR ALPHA-KETO ACID-DEPENDENT NONHEME IRON ENZYMES - STRUCTURES AND REACTIVITY OF [FE-II(L)(O(2)CCOPH)](CLO4) COMPLEXES [J].