THIOREDOXIN STRUCTURE AND MECHANISM - CONFORMATIONAL-CHANGES ON OXIDATION OF THE ACTIVE-SITE SULFHYDRYLS TO A DISULFIDE

被引：373
作者：
HOLMGREN, A
机构：
[1] Arne Holmgren, Medical Nobel Institute for Biochemistry, Department of Medical Biochemistry and Biophysics
来源：
STRUCTURE | 1995年 / 3卷 / 03期
关键词：
D O I：
10.1016/S0969-2126(01)00153-8
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：
The recent high-resolution solution structures of human and Escherichia coli thioredoxin in their oxidized and reduced states support a catalytic model of protein disulfide reduction involving binding of a target protein and nucleophilic attack by the active-site Cys32 thiolate to form a transition state mixed disulfide. © 1995 Elsevier Science Ltd. All rights reserved.
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页码：239 / 243
页数：5
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