Globins Scavenge Sulfur Trioxide Anion Radical

Gardner, Paul R.; Gardner, Daniel P.; Gardner, Alexander P.

doi:10.1074/jbc.m115.679621

Cited by 16 publications

(22 citation statements)

References 82 publications

(29 reference statements)

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“…The molecular mechanisms of sulfite antimicrobial actions have not been clearly defined. However, several plausible reactions have been proposed that are useful for a general understanding in biological systems where the oxidation of sulfite and the subsequent chain reactions provides reactive intermediates capable of adversely reacting with biological molecules [ 22 , 23 ]. Sulfite is a strong nucleophile and reacts with many biomolecules by substitution at electrophilic positions causing a myriad of potential cell damaging reactions.…”

Section: Discussionmentioning

confidence: 99%

“…plantarum showed similar and higher susceptibility to sulfites than the homofermentative LAB Streptococcus thermophilus . One possible difference in their susceptibilities may be the formation of the highly toxic sulfur trioxide anion radicals (STAR), which are known to be formed by the reaction of sulfite with H 2 O 2 [ 22 – 24 ]. All the bacteria tested in this study are known to produce variable amounts of hydrogen peroxide (H 2 O 2 ) dependent on environmental conditions [ 25 ].…”

Section: Discussionmentioning

confidence: 99%

“…Sulfite is oxidized to sulfate in mammals by the mitochondrial enzyme sulfite oxidase, found predominantly in liver and kidney cells [ 22 ]. The concentration of sulfites an individual can metabolize daily is variable based on the amount of the enzyme being produced and individual genetic and environmental conditions.…”

Section: Discussionmentioning

confidence: 99%

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Sulfites inhibit the growth of four species of beneficial gut bacteria at concentrations regarded as safe for food

et al. 2017

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Sulfites and other preservatives are considered food additives to limit bacterial contamination, and are generally regarded as safe for consumption by governmental regulatory agencies at concentrations up to 5000 parts per million (ppm). Consumption of bactericidal and bacteriostatic drugs have been shown to damage beneficial bacteria in the human gut and this damage has been associated with several diseases. In the present study, bactericidal and bacteriostatic effects of two common food preservatives, sodium bisulfite and sodium sulfite, were tested on four known beneficial bacterial species common as probiotics and members of the human gut microbiota. Lactobacillus species casei, plantarum and rhamnosus, and Streptococcus thermophilus were grown under optimal environmental conditions to achieve early log phase at start of experiments. Bacterial cultures were challenged with sulfite concentrations ranging between 10 and 3780 ppm for six hours. To establish a control, a culture of each species was inoculated into media containing no sulfite preservative. By two hours of exposure, a substantial decrease (or no increase) of cell numbers (based on OD600 readings) were observed for all bacteria types, in concentrations of sulfites between 250–500 ppm, compared to cells in sulfite free media. Further testing using serial dilution and drop plates identified bactericidal effects in concentrations ranging between 1000–3780 ppm on all the Lactobacillus species by 4 hours of exposure and bactericidal effects on S. thermophilus in 2000ppm NaHSO3 after 6 hours of exposure.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Sulfites inhibit the growth of four species of beneficial gut bacteria at concentrations regarded as safe for food

et al. 2017

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“…Yhb1 is localized in the mitochondria in anoxic conditions, while a dual cytoplasmatic/mitochondrial localization is observed in aerobic conditions [7] . It has also been recently shown to be involved in sulfur detoxification [10] . In mammals, neuroglobin it is structurally related to the globin domain and could conserve some of its functions [2] .…”

Section: Introductionmentioning

confidence: 99%

Nitric oxide prevents Aft1 activation and metabolic remodeling in frataxin-deficient yeast

Alsina¹,

Ros²,

Tamarit³

2018

Redox Biology

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Yeast frataxin homolog (Yfh1) is the orthologue of human frataxin, a mitochondrial protein whose deficiency causes Friedreich Ataxia. Yfh1 deficiency activates Aft1, a transcription factor governing iron homeostasis in yeast cells. Although the mechanisms causing this activation are not completely understood, it is assumed that it may be caused by iron-sulfur deficiency. However, several evidences indicate that activation of Aft1 occurs in the absence of iron-sulfur deficiency. Besides, Yfh1 deficiency also leads to metabolic remodeling (mainly consisting in a shift from respiratory to fermentative metabolism) and to induction of Yhb1, a nitric oxide (NO) detoxifying enzyme. In this work, we have used conditional Yfh1 mutant yeast strains to investigate the relationship between NO, Aft1 activation and metabolic remodeling. We have observed that NO prevents Aft1 activation caused by Yfh1 deficiency. This phenomenon is not observed when Aft1 is activated by iron scarcity or impaired iron-sulfur biogenesis. In addition, analyzing key metabolic proteins by a targeted proteomics approach, we have observed that NO prevents the metabolic remodeling caused by Yfh1 deficiency. We conclude that Aft1 activation in Yfh1-deficient yeasts is not caused by iron-sulfur deficiency or iron scarcity. Our hypothesis is that Yfh1 deficiency leads to the presence of anomalous iron species that can compromise iron bioavailability and activate a signaling cascade that results in Aft1 activation and metabolic remodeling.

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“…Examples of such mechanisms are well known in aerobic organisms, where enzymatic activities generating ROS and/or reactive nitrogen species (RNS) affect the function of proteins sensitive to these species. However, the sulfur-centered radicals are of significance in this regard too (48,58,76,98), adding yet another aspect to novel insights on the role of sulfur in regulation of biological processes (189). Although the sulfur-based radicals have not attracted such attention as ROS or RNS in biological studies, the ability of thiyl radicals to promote not only oxygen reduction but also nitrosylation and transnitrosylation reactions (98) certainly warrants more attention to production of these radicals in biological systems and their potential involvement in homeostatic mechanisms.…”

mentioning

confidence: 99%

Redox-Driven Signaling: 2-Oxo Acid Dehydrogenase Complexes as Sensors and Transmitters of Metabolic Imbalance

Bunik

2019

Antioxidants & Redox Signaling

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Interaction of 2-oxo acid dehydrogenase complexes with thioredoxins, peroxiredoxins and glutaredoxins mediates scavenging of the thiyl radicals and ROS generated by the complexes, underlying signaling of disproportional availability of 2-oxo acids, CoA and NAD+ in key metabolic branch points through thiol-disulfide exchange and medically important HIF, mTOR, PARP and sirtuins. High reactivity of the co-produced ROS and thiyl radicals to iron-sulfur clusters and nitric oxide, peroxynitrite reductase activity of peroxyredoxins and transnitrosylating function of thioredoxin, implicate the side reactions of 2-oxo acid dehydrogenase complexes in nitric-oxide-dependent signaling and damage.

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Globins Scavenge Sulfur Trioxide Anion Radical

Cited by 16 publications

References 82 publications

Sulfites inhibit the growth of four species of beneficial gut bacteria at concentrations regarded as safe for food

Sulfites inhibit the growth of four species of beneficial gut bacteria at concentrations regarded as safe for food

Nitric oxide prevents Aft1 activation and metabolic remodeling in frataxin-deficient yeast

Redox-Driven Signaling: 2-Oxo Acid Dehydrogenase Complexes as Sensors and Transmitters of Metabolic Imbalance

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