Abstract
Summary Thiosulfate reductase (thiosulfate-thiol sulfurtransferase, (EC 2.8.1.3) TSR) and rhodanese (thiosulfate-cyanide sulfurtransferase, (EC 2.8.1.1) RDN) activities have been identified in crude extracts from the eukaryotic green alga Chlamydomonas reinhardtii . These activities co-purified after several purification steps and no isoforms have been separated. Kinetic studies indicate that dithiols (DTE) exert a competitive inhibition on rhodanese activity, the affinity for DTE being 28-fold higher than that for cyanide. These results support the idea that both activities are mediated by the same protein. The activities are not sensitive to thiol reagents, whereas they are inhibited by specific arginine-modifying reagents. The physiological role of this enzyme could be basically the assimilation of S-sulfane by the alga.
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