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

被引:168
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
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
收藏
页码:331 / 355
页数:25
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