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Molecules 2015, 20(1), 1410-1423;

Possible Roles of Plant Sulfurtransferases in Detoxification of Cyanide, Reactive Oxygen Species, Selected Heavy Metals and Arsenate

Institute of Botany, Leibniz University Hannover, Herrenhäuserstr. 2, Hannover D-30419, Germany
Plant Breeding Division, Bangladesh Agricultural Research Institute, Joydebpur, Gazipur 1701, Bangladesh
Author to whom correspondence should be addressed.
Academic Editors: Noriyuki Nagahara and Maria Wrobel
Received: 10 November 2014 / Accepted: 9 January 2015 / Published: 14 January 2015
(This article belongs to the Special Issue Sulfur Atom: Element for Adaptation to an Oxidative Environment)
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Plants and animals have evolved various potential mechanisms to surmount the adverse effects of heavy metal toxicity. Plants possess low molecular weight compounds containing sulfhydryl groups (-SH) that actively react with toxic metals. For instance, glutathione (γ-Glu-Cys-Gly) is a sulfur-containing tripeptide thiol and a substrate of cysteine-rich phytochelatins (γ-Glu-Cys)2–11-Gly (PCs). Phytochelatins react with heavy metal ions by glutathione S-transferase in the cytosol and afterwards they are sequestered into the vacuole for degradation. Furthermore, heavy metals induce reactive oxygen species (ROS), which directly or indirectly influence metabolic processes. Reduced glutathione (GSH) attributes as an antioxidant and participates to control ROS during stress. Maintenance of the GSH/GSSG ratio is important for cellular redox balance, which is crucial for the survival of the plants. In this context, sulfurtransferases (Str), also called rhodaneses, comprise a group of enzymes widely distributed in all phyla, paving the way for the transfer of a sulfur atom from suitable sulfur donors to nucleophilic sulfur acceptors, at least in vitro. The best characterized in vitro reaction is the transfer of a sulfane sulfur atom from thiosulfate to cyanide, leading to the formation of sulfite and thiocyanate. Plants as well as other organisms have multi-protein families (MPF) of Str. Despite the presence of Str activities in many living organisms, their physiological role has not been clarified unambiguously. In mammals, these proteins are involved in the elimination of cyanide released from cyanogenic compounds. However, their ubiquity suggests additional physiological functions. Furthermore, it is speculated that a member of the Str family acts as arsenate reductase (AR) and is involved in arsenate detoxification. In summary, the role of Str in detoxification processes is still not well understood but seems to be a major function in the organism. View Full-Text
Keywords: arsenate; arsenate reductase; cyanide; rhodanese; sulfurtransferase arsenate; arsenate reductase; cyanide; rhodanese; sulfurtransferase

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Most, P.; Papenbrock, J. Possible Roles of Plant Sulfurtransferases in Detoxification of Cyanide, Reactive Oxygen Species, Selected Heavy Metals and Arsenate. Molecules 2015, 20, 1410-1423.

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