A bis-cyclodextrin diselenide with glutathione peroxidase-like activity

被引：79

作者：

Liu, JQ

Luo, GM ^{[1
]}

Ren, XJ

Mu, Y

Bai, Y

Shen, JC

机构：

[1] Jilin Univ, Key Lab Mol Enzymol & Engn, Changchun 130023, Peoples R China

[2] Univ PLA, Changchun 130026, Peoples R China

[3] Jilin Univ, Key Lab Supramol Struct & Spect, Changchun 130023, Peoples R China

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 2000年 / 1481卷 / 02期

关键词：

beta-cyclodextrin; glutathione peroxidase; imitating enzyme; selenium;

D O I：

10.1016/S0167-4838(00)00130-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A diselenide, 2,2'-diseleno-bis-beta-cyclodextrin (2-SeCD), was synthesized to imitate the antioxidant enzyme glutathione peroxidase (GPX). The GPX mimic accepts a variety of hydroperoxides as substrates. The GPX activities, reduction of H2O2, tert-butyl hydroperoxide and cumenyl hydroperoxide by glutathione, are 7.4, 4.5 and 10.2 U/mu mol, respectively. In contrast to ebselen (PZ51), the diselenide displays high GPX-like activity. The reduction of hydroperoxide by glutathione in the presence of a radical trap shows that the mimic catalyzes the reaction via a non-radical mechanism. A ping-pong mechanism was observed in the steady-state kinetic studies of the 2-SeCD-catalyzed reaction. (C) 2000 Elsevier Science B.V. All rights reserved.

引用

页码：222 / 228

页数：7

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