Effect of mercury(II) traces on catalytic activity of peanut and horseradish peroxidasesстатья
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Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
Авторы:
Bagirova N.A.a ,
Muginova S.V.a ,
Shekhovtsova T.N.a.c ,
Gazaryan I.G.a ,
Van Huystee R.B.b
Журнал:
Analytical Letters
Том:
39
Номер:
3
Год издания:
2006
Издательство:
Marcel Dekker Inc.
Местоположение издательства:
United States
Первая страница:
521
Последняя страница:
541
DOI:
10.1080/00032710500536137
Аннотация:
Mercury(II) in the range of 0.1-1 μg L-1 concentrations was found to be a much more efficient inhibitor of native peanut peroxidase (PNP) than of horseradish peroxidase (HRP) in the reaction of o-dianisidine oxidation with hydrogen peroxide. The possible reason for the different degree of mercury(II) effects on the catalytic activity of both enzymes was studied. It was shown that the different number of glycans in PNP and HRP molecules (three and eight, respectively), or their absence in the molecule of wild-type recombinant horseradish peroxidase refolded from E. coli inclusion bodies (recHRP), does not play a significant role in the effects caused by mercury(II). The efficient inhibition of PNP by mercury(II) in the absence of any other additives (for example, thiourea) originates from a greater mobility of the distal calcium ion in the enzyme molecule. A model scheme for the interaction of the studied plant peroxidases with mercury(II) was proposed. The PNP-based enzymatic method for mercury(II) determination with cmin = 0.04 μg L-1 (0.2 nmol L-1) was developed and the possibility of PNP application for analysis of different samples was demonstrated. Copyright © Taylor & Francis Group, LLC.
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