INACTIVATION OF THIOREDOXIN BY SULFITE IONS

被引：32

作者：

WURFEL, M

HABERLEIN, I

FOLLMANN, H

机构：

[1] Fachbereich Biologie-Chemie der Universität, D-3500 Kassel

来源：

FEBS LETTERS | 1990年 / 268卷 / 01期

关键词：

Enzyme activation; NADP-malate dehydrogenase; Sulfitolysis; Thioredoxin; E; coli; Thioredoxin-S-sulfonate;

D O I：

10.1016/0014-5793(90)80994-T

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：

Oxidized thioredoxin undergoes sulfitolysis of its single disulfide bond at low concentrations of sulfite ions and protein and in the absence of denaturing agents. The reaction, which has an optimum at pH 8, was studied using [35S]sulfite and E. coli thioredoxin as model. The product, thioredoxin-S-sulfonate, has a half-life of several hours in solution. It is unable to activate chloroplast NADP malate dehydrogenase. Thioredoxin sulfitolysis may therefore be a physiologically important factor in mediating the phytotoxic effects ofsulfur dioxide in plants. © 1990.

引用

页码：146 / 148

页数：3

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