Inactivation of thioredoxin by sulfite ions.
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 of sulfur dioxide in plants.
Fachbereich Biologie-Chemie der Universität, Kassel, FRG.
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Würfel
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Häberlein
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Follmann
D001426:Bacterial Proteins / Q000037:antagonists & inhibitors*; D055598:Chemical Phenomena; D002621:Chemistry; D004926:Escherichia coli / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D013447:Sulfites / Q000494:pharmacology*; D013879:Thioredoxins / Q000037:antagonists & inhibitors*
D001426:Bacterial Proteins; D013447:Sulfites; D013879:Thioredoxins