Coordination Chemistry Reviews
190–192 (1999) 331–355
Structural properties of the nickel ions in
urease: novel insights into the catalytic and
inhibition mechanisms
Stefano Ciurli
a,
*, Stefano Benini
b
, Wojciech R. Rypniewski
b
,
Keith S. Wilson
c
, Silvia Miletti
a
, Stefano Mangani
d
a
Institute of Agricultural Chemistry, Uniersity of Bologna, Viale Berti Pichat 10,
I -40127 Bologna, Italy
b
European Molecular Biology Laboratory, c /o DESY, Notkestraße 85, D-22603 Hamburg, Germany
c
Department of Chemistry, Uniersity of York, Heslington, York YO15DD, UK
d
Department of Chemistry, Uniersity of Siena, Pian dei Mantellini 44, I -53100 Siena, Italy
Accepted 13 March 1999
Contents
Abstract .................................................... 331
1. Biological background ......................................... 332
2. Spectroscopic investigations of the urease active site structure .................. 333
3. Crystallographic studies of the native enzyme ............................ 334
4. Crystallographic studies of urease mutants .............................. 341
5. Crystallographic studies of urease – inhibitor complexes ...................... 345
6. Crystallographic study of a transition state analogue bound to urease .............. 348
7. A novel proposal for the urease mechanism ............................. 350
References .................................................. 353
Abstract
This work provides a comprehensive critical summary of urease spectroscopy, crystallogra-
phy, inhibitor binding, and site-directed mutagenesis, with special emphasis given to the
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Abbreiations: JBU, jack bean urease; KAU, Klebsiella aerogenes urease; BPU, Bacillus pasteurii
urease; -ME, -mercaptoethanol; PPD, phenylphosphorodiamidate; AHA, acetohydroxamic acid;
XAS, X-ray absorption spectroscopy; EXAFS, extended X-ray absorption fine structure; CD, circular
dichroism; MCD, magnetic circular dichroism.
* Corresponding author. Tel.: +39-051-259794; fax: +39-051-243362.
E-mail address: sciurli@agrsci.unibo.it (S. Ciurli)
0010-8545/99/$ - see front matter © 1999 Elsevier Science S.A. All rights reserved.
PII:S0010-8545(99)00093-4