Inactivation of urease by 1,4-benzoquinone: chemistry at the protein surface-Reference-Cited by-同舟云学术

Inactivation of urease by 1,4-benzoquinone: chemistry at the protein surface

Published:2016 Issue:13 Volume:45 Page:5455-5459
ISSN:1477-9226
Container-title:Dalton Transactions
language:en
Short-container-title:Dalton Trans.

Author:

Mazzei L.¹²³⁴⁵,Cianci M.⁶⁷⁸^ORCID,Musiani F.¹²³⁴⁵,Ciurli S.¹²³⁴⁵

Affiliation:

1. Laboratory of bioinorganic Chemistry

2. Department of Pharmacy and Biotechnology

3. University of Bologna

4. Bologna

5. Italy

6. European Molecular Biology Laboratory

7. 22607 Hamburg

8. Germany

Abstract

The high activity of urease, a Ni(ii) enzyme, has several adverse effects on human health and agriculture, and its modulation needs the use of inhibitors.

Publisher

Royal Society of Chemistry (RSC)

Subject

Inorganic Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2016/DT/C6DT00652C

Reference32 articles.

1. Chemistry of Ni2+ in Urease: Sensing, Trafficking, and Catalysis

2. Nonredox Nickel Enzymes

3. The Emerging Role of Urease as a General Microbial Virulence Factor

4. S. Kiss and M.Simihaian, Improving efficiency of urea fertilizers by inhibition of soil urease activity, Kluwer Academic Publishers, Dordrecht, The Netherlands, 2002

5. A new proposal for urease mechanism based on the crystal structures of the native and inhibited enzyme from Bacillus pasteurii: why urea hydrolysis costs two nickels

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