XAS investigation of the nickel active site structure in Escherichia coli glyoxalase I

被引：21

作者：

Davidson, G

Clugston, SL

Honek, JF

Maroney, MJ ^{[1
]}

机构：

[1] Univ Massachusetts, Dept Chem, Amherst, MA 01003 USA

[2] Univ Waterloo, Dept Chem, Waterloo, ON N2L 3G1, Canada

来源：

INORGANIC CHEMISTRY | 2000年 / 39卷 / 14期

关键词：

D O I：

10.1021/ic0001208

中图分类号：

O61 [无机化学];

学科分类号：

070301 ; 081704 ;

摘要：

Escherichia coli glyoxalase I (GU) is the first example of an isomerase that is maximally activated by Ni2+. In contrast with GlxI enzymes from other sources that are Zn enzymes, E. coli GlxI is not active with Zn bound. Structural details from X-ray absorption spectroscopic analyses are reported for the active site Ni center and the Zn-substituted enzyme. The available data regarding the structure of the active Ni site are consistent with a six-coordinate Ni(Glu)(2)(His)(2)(OH2)(2) site in the enzyme.

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页码：2962 / +

页数：3

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