Possible roles of plant sulfurtransferases in detoxification of cyanide, reactive oxygen species, selected heavy metals and arsenate

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dc.identifier.uri http://dx.doi.org/10.15488/642
dc.identifier.uri http://www.repo.uni-hannover.de/handle/123456789/666
dc.contributor.author Most, Parvin
dc.contributor.author Papenbrock, Jutta
dc.date.accessioned 2016-11-03T09:29:55Z
dc.date.available 2016-11-03T09:29:55Z
dc.date.issued 2015
dc.identifier.citation Most, Parvin; Papenbrock, Jutta: Possible roles of plant sulfurtransferases in detoxification of cyanide, reactive oxygen species, selected heavy metals and arsenate. In: Molecules 20 (2015), Nr. 1, S 1410-1423. DOI: http://dx.doi.org/10.3390/molecules20011410
dc.description.abstract 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. eng
dc.description.sponsorship DAAD
dc.language.iso eng
dc.publisher Basel : MDPI AG
dc.relation.ispartofseries Molecules 20 (2015), Nr. 1
dc.rights CC BY-NC-SA 4.0
dc.rights.uri https://creativecommons.org/licenses/by-nc-sa/4.0/
dc.subject Arsenate eng
dc.subject Arsenate reductase eng
dc.subject Cyanide eng
dc.subject Rhodanese eng
dc.subject Sulfurtransferase eng
dc.subject arsenic acid eng
dc.subject arsenic acid derivative eng
dc.subject cyanide eng
dc.subject heavy metal eng
dc.subject reactive oxygen metabolite eng
dc.subject sulfurtransferase eng
dc.subject drug inactivation eng
dc.subject enzymology eng
dc.subject metabolism eng
dc.subject plant eng
dc.subject Arsenates eng
dc.subject Cyanides eng
dc.subject Inactivation, Metabolic eng
dc.subject Metals, Heavy eng
dc.subject Plants eng
dc.subject Reactive Oxygen Species eng
dc.subject Sulfurtransferases eng
dc.subject.ddc 500 | Naturwissenschaften ger
dc.subject.ddc 540 | Chemie ger
dc.title Possible roles of plant sulfurtransferases in detoxification of cyanide, reactive oxygen species, selected heavy metals and arsenate
dc.type article
dc.type Text
dc.relation.issn 1420-3049
dc.relation.doi http://dx.doi.org/10.3390/molecules20011410
dc.bibliographicCitation.issue 1
dc.bibliographicCitation.volume 20
dc.bibliographicCitation.firstPage 1410
dc.bibliographicCitation.lastPage 1423
dc.description.version publishedVersion
tib.accessRights frei zug�nglich


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