Inactivation of thioredoxin by sulfite ions

FEBS Letters

Häberlein, Ingo¹  Follmann, Hartmut¹  Würfel, Martina¹ 

[1] Fachbereich Biologie-Chemie der Universität, Heinrich-Plettstrasse 40, D-3500 Kassel, FRG

关键词: Enzyme activation;    NADP-malate dehydrogenase;    Sulfitolysis;    Thioredoxin;    E. coli;    Thioredoxin-S-sulfonate;   

DOI  :  10.1016/0014-5793(90)80994-T

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown