Structural properties of the nickel ions in urease: novel insights into the catalytic and inhibition mechanisms

被引：167

作者：

Ciurli, S

Benini, S

Rypniewski, WR

Wilson, KS

Miletti, S

Mangani, S

机构：

[1] Univ Bologna, Inst Agr Chem, I-40127 Bologna, Italy

[2] DESY, European Mol Biol Lab, D-22603 Hamburg, Germany

[3] Univ York, Dept Chem, York YO1 5DD, N Yorkshire, England

[4] Univ Siena, Dept Chem, I-53100 Siena, Italy

来源：

COORDINATION CHEMISTRY REVIEWS | 1999年 / 190卷

关键词：

urease spectroscopy; site-directed mutagenesis; inhibitor binding;

D O I：

10.1016/S0010-8545(99)00093-4

中图分类号：

O61 [无机化学];

学科分类号：

070301 ; 081704 ;

摘要：

This work provides a comprehensive critical summary of urease spectroscopy, crystallography, inhibitor binding, and site-directed mutagenesis, with special emphasis given to the relationships between the structural Features of the Ni-containing active site and the physico-chemical and biochemical properties of this metallo-enzyme. In addition, the recently determined structure of a complex between urease and a transition state analogue is discussed as it leads to a novel, thought-provoking proposal for the enzyme mechanism. (C) 1999 Elsevier Science S.A. All rights reserved.

引用

页码：331 / 355

页数：25

共 84 条

[1] THE NICKEL ION ENVIRONMENT IN JACK BEAN UREASE [J].