Specific anion effects on urease activity: A Hofmeister study

被引：4

作者：

Acar, Mert ^{[1
,2
]}

Tatini, Duccio ^{[1
,2
]}

Budroni, Marcello A. ^{[3
]}

Ninham, Barry W. ^{[4
]}

Rustici, Mauro ^{[3
]}

Rossi, Federico ^{[5
]}

Lo Nostro, Pierandrea ^{[1
,2
]}

机构：

[1] Univ Florence, Dept Chem Ugo Schiff, I-50019 Sesto Fiorentino, Firenze, Italy

[2] Univ Florence, CSGI, I-50019 Sesto Fiorentino, Firenze, Italy

[3] Univ Sassari, Dept Chem, Pharm, I-07100 Sassari, Italy

[4] Australian Natl Univ, Res Sch Phys Sci & Engn, Dept Appl Math, Canberra, ACT 0200, Australia

[5] Univ Siena, Dept Earth Environm & Phys Sci DEEP Sci, Siena, Italy

来源：

COLLOIDS AND SURFACES B-BIOINTERFACES | 2024年 / 236卷

关键词：

Hofmeister series; Kosmotropicity; Chaotropicity; Enzymatic activity; Urease; JACK BEAN UREASE; KLEBSIELLA-AEROGENES UREASE; AQUEOUS-SOLUTIONS; OPTICAL-ROTATION; ION-BINDING; INHIBITION; SERIES; WATER; PH; ELECTROLYTES;

D O I：

10.1016/j.colsurfb.2024.113789

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

The effects of a range of electrolytes on the hydrolysis of urea by the enzyme urease is explored. The autocatalytic behavior of urease in unbuffered solutions and its pH clock reactions are studied. The concentration dependence of the experimental variables is analyzed in terms of specific ion-enzyme interactions and hydration. The results offer insights into the molecular mechanisms of the enzyme, and on the nature of its interactions with the electrolytes. We found that urease can tolerate mild electrolytes in its environment, while it is strongly inhibited by both strong kosmotropic and strong chaotropic anions. This study may cast light on an alternative therapy for Helicobacter pylori infections and contribute to the design of innovative materials and provide new approaches for the modulation of the enzymatic activity.

引用

页数：8

共 78 条

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