Superoxide generated from the glutathione-mediated reduction of selenite damages the iron-sulfur cluster of chloroplastic ferredoxin

Copyright © 2016 Elsevier Masson SAS. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant physiology and biochemistry : PPB. - 1991. - 106(2016) vom: 13. Sept., Seite 228-35
1. Verfasser: Fisher, Brian (VerfasserIn)
Weitere Verfasser: Yarmolinsky, Dmitry, Abdel-Ghany, Salah, Pilon, Marinus, Pilon-Smits, Elizabeth A, Sagi, Moshe, Van Hoewyk, Doug
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2016
Zugriff auf das übergeordnete Werk:Plant physiology and biochemistry : PPB
Schlagworte:Journal Article Ferredoxin Iron-sulfur cluster Oxidative stress Selenium Superoxide Ferredoxins Iron-Sulfur Proteins Superoxides 11062-77-4 mehr... NADP 53-59-8 Cytochromes c 9007-43-6 Ferredoxin-NADP Reductase EC 1.18.1.2 Sulfite Reductase (Ferredoxin) EC 1.8.7.1 Selenious Acid F6A27P4Q4R Glutathione GAN16C9B8O
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100 1 |a Fisher, Brian  |e verfasserin  |4 aut 
245 1 0 |a Superoxide generated from the glutathione-mediated reduction of selenite damages the iron-sulfur cluster of chloroplastic ferredoxin 
264 1 |c 2016 
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500 |a Date Completed 27.03.2017 
500 |a Date Revised 30.09.2020 
500 |a published: Print-Electronic 
500 |a Citation Status MEDLINE 
520 |a Copyright © 2016 Elsevier Masson SAS. All rights reserved. 
520 |a Selenium assimilation in plants is facilitated by several enzymes that participate in the transport and assimilation of sulfate. Manipulation of genes that function in sulfur metabolism dramatically affects selenium toxicity and accumulation. However, it has been proposed that selenite is not reduced by sulfite reductase. Instead, selenite can be non-enzymatically reduced by glutathione, generating selenodiglutathione and superoxide. The damaging effects of superoxide on iron-sulfur clusters in cytosolic and mitochondrial proteins are well known. However, it is unknown if superoxide damages chloroplastic iron-sulfur proteins. The goals of this study were twofold: to determine whether decreased activity of sulfite reductase impacts selenium tolerance in Arabidopsis, and to determine if superoxide generated from the glutathione-mediated reduction of selenite damages the iron-sulfur cluster of ferredoxin. Our data demonstrate that knockdown of sulfite reductase in Arabidopsis does not affect selenite tolerance or selenium accumulation. Additionally, we provide in vitro evidence that the non-enzymatic reduction of selenite damages the iron-sulfur cluster of ferredoxin, a plastidial protein that is an essential component of the photosynthetic light reactions. Damage to ferredoxin's iron-sulfur cluster was associated with formation of apo-ferredoxin and impaired activity. We conclude that if superoxide damages iron-sulfur clusters of ferredoxin in planta, then it might contribute to photosynthetic impairment often associated with abiotic stress, including toxic levels of selenium 
650 4 |a Journal Article 
650 4 |a Ferredoxin 
650 4 |a Iron-sulfur cluster 
650 4 |a Oxidative stress 
650 4 |a Selenium 
650 4 |a Superoxide 
650 7 |a Ferredoxins  |2 NLM 
650 7 |a Iron-Sulfur Proteins  |2 NLM 
650 7 |a Superoxides  |2 NLM 
650 7 |a 11062-77-4  |2 NLM 
650 7 |a NADP  |2 NLM 
650 7 |a 53-59-8  |2 NLM 
650 7 |a Cytochromes c  |2 NLM 
650 7 |a 9007-43-6  |2 NLM 
650 7 |a Ferredoxin-NADP Reductase  |2 NLM 
650 7 |a EC 1.18.1.2  |2 NLM 
650 7 |a Sulfite Reductase (Ferredoxin)  |2 NLM 
650 7 |a EC 1.8.7.1  |2 NLM 
650 7 |a Selenious Acid  |2 NLM 
650 7 |a F6A27P4Q4R  |2 NLM 
650 7 |a Glutathione  |2 NLM 
650 7 |a GAN16C9B8O  |2 NLM 
700 1 |a Yarmolinsky, Dmitry  |e verfasserin  |4 aut 
700 1 |a Abdel-Ghany, Salah  |e verfasserin  |4 aut 
700 1 |a Pilon, Marinus  |e verfasserin  |4 aut 
700 1 |a Pilon-Smits, Elizabeth A  |e verfasserin  |4 aut 
700 1 |a Sagi, Moshe  |e verfasserin  |4 aut 
700 1 |a Van Hoewyk, Doug  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t Plant physiology and biochemistry : PPB  |d 1991  |g 106(2016) vom: 13. Sept., Seite 228-35  |w (DE-627)NLM098178261  |x 1873-2690  |7 nnns 
773 1 8 |g volume:106  |g year:2016  |g day:13  |g month:09  |g pages:228-35 
856 4 0 |u http://dx.doi.org/10.1016/j.plaphy.2016.05.004  |3 Volltext 
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