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

Fisher, Brian D.; Yarmolinsky, Dmitry; Abdel‐Ghany, Salah E.; Pilon, Marinus; Pilon-Smits, Elizabeth A. H.; Sagi, Moshe; Hoewyk, Doug Van

doi:10.1016/j.plaphy.2016.05.004

Cited by 29 publications

(23 citation statements)

References 53 publications

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“…The iron-sulfur clusters were the primary intracellular targets of metal ion toxicity. Higher concentrations of metal ion led to total disintegration of the Fe-S cluster in central catabolic and biosynthetic pathways, evidently displacing iron atoms [24,28,29]. Some iron-containing enzymes are inhibited by nickel, with some shown to have nickel replacing the active metal [26].…”

Section: Discussionmentioning

confidence: 99%

Responses of Acidithiobacillus thiooxidans A01 to Individual and Joint Nickel (Ni2+) and Ferric (Fe3+)

et al. 2019

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Acidithiobacillus thiooxidans A01 is widely used in bioleaching processes and commonly thrives in most metal-rich environments. However, interactions between different heavy metals remain obscure. In this study, we elaborated the effect of ferric iron on the growth and gene expression of At. thiooxidans A01 under the stress of nickel. The results showed that 600 mM Ni 2+ completely inhibited the growth and sulfur metabolism of At. thiooxidans A01. However, trace amounts of Fe 3+ (0.5 mM) facilitated the growth of At. thiooxidans A01 in the presence of 600 mM Ni 2+ . With the addition of 5 mM Fe 3+ , the maximum cell density reached 1.84 × 10 8 cell/mL, and pH value was 0.95. In addition, metal resistance-related and sulfur metabolism genes were significantly up regulated with extra ferric iron. Taking the whole process into account, the promoting effect of Fe 3+ addition can be attributed to the following: (1) alleviation of the effects of Ni 2+ toxicity and restoring the growth of At. thiooxidans A01, (2) a choice of multiple pathways to export nickel ion and producing precursor of chelators of heavy metals. This can suggest that microorganisms may widely exhibit metabolic activity in iron-rich environments with heavy metals. Our study will facilitate the technique development for the processing of ore bodies with highly challenging ore compositions.

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Section: Discussionmentioning

confidence: 99%

Responses of Acidithiobacillus thiooxidans A01 to Individual and Joint Nickel (Ni2+) and Ferric (Fe3+)

et al. 2019

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“…Oxidative stress and apoptosis occurs when mammalian cells are treated with SeO 3 2− [124,134,135,136,137,138,139,140,141,142,143]. Superoxide (O 2 − •) is known to be produced when SeO 3 2− reacts with GSH [144]. In Vitro evidence demonstrated that non-enzymatic reduction of SeO 3 2− by GSH rapidly yields GSSeSG and O 2 − • [135,144,145,146,147].…”

Section: Unanswered Questionsmentioning

confidence: 99%

“…Superoxide (O 2 − •) is known to be produced when SeO 3 2− reacts with GSH [144]. In Vitro evidence demonstrated that non-enzymatic reduction of SeO 3 2− by GSH rapidly yields GSSeSG and O 2 − • [135,144,145,146,147]. Additionally, apoptosis is known to be induced by ROS like O 2 − • [3].…”

Section: Unanswered Questionsmentioning

confidence: 99%

Biological Chemistry of Hydrogen Selenide

Cupp‐Sutton

Ashby

2016

Antioxidants

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There are no two main-group elements that exhibit more similar physical and chemical properties than sulfur and selenium. Nonetheless, Nature has deemed both essential for life and has found a way to exploit the subtle unique properties of selenium to include it in biochemistry despite its congener sulfur being 10,000 times more abundant. Selenium is more easily oxidized and it is kinetically more labile, so all selenium compounds could be considered to be “Reactive Selenium Compounds” relative to their sulfur analogues. What is furthermore remarkable is that one of the most reactive forms of selenium, hydrogen selenide (HSe− at physiologic pH), is proposed to be the starting point for the biosynthesis of selenium-containing molecules. This review contrasts the chemical properties of sulfur and selenium and critically assesses the role of hydrogen selenide in biological chemistry.

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“…Both photosystem (PS) II and PSI generate ROS during HL stress. Superoxide can damage the iron-sulfur clusters in proteins found predominantly in PSI [3] and ferredoxin [4]. Compared to PSI, however, PSII is more susceptible to photoinhibition, and includes the production of singlet oxygen and superoxide [5].…”

Section: Introductionmentioning

confidence: 99%

Proteasome inhibition rapidly exacerbates photoinhibition and impedes recovery during high light stress in Chlamydomonas reinhardtii

et al. 2020

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Background: Proteasomes remove regulatory proteins in eukaryotic cells, and control a variety of plant processes. Proteasomes are localized to the cytosol and nuclear, but their role in plant biology has recently been extended to chloroplasts, where it regulates TOC complex. This is turn controls the import of nuclear-encoded chloroplastic proteins, which remodels the chloroplast proteome and facilitates proper developmental transitions. Proteasomal regulation of the TOC complex also alleviates stressors that generate reactive oxygen species. These recent advances motivated us to determine if proteasome inhibition rapidly alters photosynthetic processes stemming from photoinhibition induced by high light. Results: The short-term effects of proteasome inhibition on photosystem II during light stress was measured in Chlamydomonas reinhardtii, which allowed the dual monitoring of both chlorophyll fluorescence and cell viability. After 48 h at low light, proteasome inhibition did not affect viability or photochemistiry, but decreased cell concentration and increased cell volume. Two hours of high light stress impaired the efficiency of photosystem II in proteasome-inhibited cells, as determined by a decrease in Fv/Fm and the electron transport rate. Elevated photoinhibition in proteasome inhibited cells was not caused by a decrease in cell viability or chlorophyll content. Recovery from photoinhibition was attenuated in MG132-treated cells, and suppressed growth of a reestablished culture. Proteasome inhibition decreased de novo protein synthesis, which possibly constrained the ability to remodel the plastid proteome, and thus hampering the ability to adjust to high light stress. Conclusion: The proteasome is implicated in protecting photosystem II from photoinhibition. In addition to high light stress, other stressors-including metals, drought, and salt-are also known to generate reactive oxygen species localized to the chloroplast. Therefore, proteasome maintenance in plants may help protect photosynthesis during abiotic stress, which could increase crop yield during adverse conditions.

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

Cited by 29 publications

References 53 publications

Responses of Acidithiobacillus thiooxidans A01 to Individual and Joint Nickel (Ni2+) and Ferric (Fe3+)

Responses of Acidithiobacillus thiooxidans A01 to Individual and Joint Nickel (Ni2+) and Ferric (Fe3+)

Biological Chemistry of Hydrogen Selenide

Proteasome inhibition rapidly exacerbates photoinhibition and impedes recovery during high light stress in Chlamydomonas reinhardtii

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