Molecular details of urease inhibition by boric acid: Insights into the catalytic mechanism

被引：139

作者：

Benini, S

Rypniewski, WR

Wilson, KS

Mangani, S

Ciurli, S

机构：

[1] Univ Bologna, Dept Agro Environm Sci & Technol, I-40127 Bologna, Italy

[2] Univ York, York Struct Biol Lab, York YO10 5DD, N Yorkshire, England

[3] Polish Acad Sci, Inst Bioorgan Chem, Poznan, Poland

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

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2004年 / 126卷 / 12期

关键词：

D O I：

10.1021/ja049618p

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The structure of the complex of urease, a Ni-containing metalloenzyme, with boric acid was determined at 2.10 Å resolution. The complex shows the unprecedented binding mode of the competitive inhibitor to the dinuclear metal center, with the B(OH)3 molecule bridging the Ni ions and leaving in place the bridging hydroxide. Boric acid can be considered a substrate analogue of urea, and the structure supports the proposal that the Ni-bridging hydroxide acts as the nucleophile in the enzymatic process of urea hydrolysis. Copyright © 2004 American Chemical Society.

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页码：3714 / 3715

页数：2

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