Cyanide Detoxification Research Articles

Physicochemical and thermodynamic properties of purified rhodanese from A. welwitschiae LOT1 and the cyanide detoxification potential of the enzyme.

Rhodanese, the primary cyanide-detoxifying enzyme, plays a crucial role in mitigating the harmful effects of cyanide present in various industrial waste materials, such as battery manufacturing effluents. The bioremediation of cyanide-contaminated environments relies on efficient detoxification mechanisms, making rhodanese a valuable enzyme for biotechnological applications. This research aimed to investigate the biochemical properties of purified rhodanese produced by Aspergillus welwitschiae LOT1, a fungal strain with promising cyanide detoxification capabilities. The purified rhodanese was obtained through fermentation, precipitation, and chromatographic separations, resulting in a homogeneous band of approximately 58kDa with a specific activity of 374 RU/mg, 28-fold purification, and 14% recovery. The enzyme exhibited optimal cyanide detoxification at pH 7 and 60°C, with stability observed between 30 and 50°C and pH 8-10. All metal ions examined except for Cu2+ enhanced the cyanide-degrading ability of rhodanese. Notably, the enzyme demonstrated a high substrate preference for Na2S2O3 and followed a first-order kinetic model and free energy, ΔG of 61.3kJ/mol, making it a promising candidate for biotechnological applications. Overall, this study provides valuable insights into the biochemical properties of rhodanese from A. welwitschiae LOT1, highlighting its potential for efficient cyanide detoxification and bioremediation.

Plant Cyanogenic-Derived Metabolites and Herbivore Counter-Defences.

The release of cyanide from cyanogenic precursors is the central core of the plant defences based on the cyanogenesis process. Although cyanide is formed as a coproduct of some metabolic routes, its production is mostly due to the degradation of cyanohydrins originating from cyanogenic glycosides in cyanogenic plants and the 4-OH-ICN route in Brassicaceae. Cyanohydrins are then hydrolysed in a reversible reaction generating cyanide, being both, cyanohydrins and cyanide, toxic compounds with potential defensive properties against pests and pathogens. Based on the production of cyanogenic-derived molecules in response to the damage caused by herbivore infestation, in this review, we compile the actual knowledge of plant cyanogenic events in the plant-pest context. Besides the defensive potential, the mode of action, and the targets of the cyanogenic compounds to combat phytophagous insects and acari, special attention has been paid to arthropod responses and the strategies to overcome the impact of cyanogenesis. Physiological and behavioural adaptations, as well as cyanide detoxification by β-cyanoalanine synthases, rhodaneses, and cyanases are common ways of phytophagous arthropods defences against the cyanide produced by plants. Much experimental work is needed to further understand the complexities and specificities of the defence-counter-defence system to be applied in breeding programs.

Structural and functional characterization of sulfurtransferase from Frondihabitans sp. PAMC28461.

Sulfurtransferases transfer of sulfur atoms from thiols to acceptors like cyanide. They are categorized as thiosulfate sulfurtransferases (TSTs) and 3-mercaptopyruvate sulfurtransferases (MSTs). TSTs transfer sulfur from thiosulfate to cyanide, producing thiocyanate. MSTs transfer sulfur from 3-mercaptopyruvate to cyanide, yielding pyruvate and thiocyanate. The present study aimed to isolate and characterize the sulfurtransferase FrST from Frondihabitans sp. PAMC28461 using biochemical and structural analyses. FrST exists as a dimer and can be classified as a TST rather than an MST according to sequence-based clustering and enzyme activity. Furthermore, the discovery of activity over a wide temperature range and the broad substrate specificity exhibited by FrST suggest promising prospects for its utilization in industrial applications, such as the detoxification of cyanide.

Impacto de la concentración de cobre en la detoxificaciónde soluciones cianuradas

There are four known methods to treat solutions with high cyanide content: natural degradation, chemical oxidation, precipitation and biological degradation. This research is carried out within the framework of chemical oxidation, with the objective of demonstrating the detoxification of cyanide with hydrogen peroxide; and having copper as a catalyst in cyanide solutions. The effect of copper concentrations of 4 was evaluated; 5; 6 and 7 ppm to reduce the levels of free cyanide in the effluent solutions of a mining plant. The average cyanide concentrations of the solutions at the inlet and outlet were reported, concluding that the copper concentration of 7 ppm obtained the best results, reducing cyanide levels from 48.31 ppm to 0.018 ppm; which is within the Maximum Permissible Limits (MPL) given by the MINAM, which corresponds to 0.8 mg/L on an annual average and 1 mg/L at any time.

Bacterial tolerance and detoxification of cyanide, arsenic and heavy metals: Holistic approaches applied to bioremediation of industrial complex wastes.

Cyanide is a highly toxic compound that is found in wastewaters generated from different industrial activities, such as mining or jewellery. These residues usually contain high concentrations of other toxic pollutants like arsenic and heavy metals that may form different complexes with cyanide. To develop bioremediation strategies, it is necessary to know the metabolic processes involved in the tolerance and detoxification of these pollutants, but most of the current studies are focused on the characterization of the microbial responses to each one of these environmental hazards individually, and the effect of co-contaminated wastes on microbial metabolism has been hardly addressed. This work summarizes the main strategies developed by bacteria to alleviate the effects of cyanide, arsenic and heavy metals, analysing interactions among these toxic chemicals. Additionally, it is discussed the role of systems biology and synthetic biology as tools for the development of bioremediation strategies of complex industrial wastes and co-contaminated sites, emphasizing the importance and progress derived from meta-omic studies.

New Insights on the Role of ß-Cyanoalanine Synthase CAS-C1 in Root Hair Elongation through Single-Cell Proteomics

(1) Background: Root hairs are specialized structures involved in water and plant nutrient uptake. They elongate from epidermal cells following a complex developmental program. ß-cyanoalanine synthase (CAS), which is mainly involved in hydrogen cyanide (HCN) detoxification in Arabidopsis thaliana, plays a role in root hair elongation, as evidenced by the fact that cas-c1 mutants show a severe defect in root hair shape. In addition to root hairs, CAS C1 is expressed in the quiescent center and meristem. (2) Methods: To identify its role in root hair formation, we conducted single-cell proteomics analysis by isolating root hair cells using Fluorescence-activated Cell Sorting (FACS) from wild-type and cas-c1 mutants. We also analyzed the presence of S-cyanylation, a protein post-translational modification (PTM) mediated by HCN and affecting cysteine residues and protein activity in proteins of wild type and cas-c1 mutants. (3) Results and Conclusions: We have found that the cas-c1 mutation has no visible effect on quiescent center or meristem root tissue, in both control and nutrient-deprivation conditions. We have identified more than 3900 proteins in root hairs and we have found that several proteins involved in root hair development, related to the receptor kinase FERONIA signaling and DNA methylation, are modified by S-cyanylation.

Cobalt, age and capacity of cyanide detoxification in children affected by konzo / Kahemba, DR Congo

Cobalt, age and capacity of cyanide detoxification in children affected by konzo / Kahemba, DR Congo

First insight into the natural biodegradation of cyanide in a gold tailings environment enriched in cyanide compounds

The disposal of mining wastes that contain cyanide are dumped in tailings from gold extraction is a public concern in mining countries such as South Africa. Many studies have shown the potential of microorganisms to degrade cyanide. However, no in-situ exploration, in tailings contaminated with cyanide, of the capability of indigenous microorganisms to act as a natural barrier for cyanide attenuation has been performed. Here we aim to combine geochemical and metagenomics techniques to reveal the genomic machinery of indigenous bacteria to degrade cyanide in gold tailings. Indigenous bacteria (i.e., Alicyclobacillus, Sulfobacillus, Acinetobacter, Achromobacter, and among others) pose the genomic machinery to trigger hydrolytic cyanide degradation using enzymes such as nitrilase, nitrile hydratase (Nhase) and thiocyanate. It seems that the lack of nitrogen sources induces the use of cyanide, which would contribute to its natural attenuation in the gold tailings. Therefore, the bacteria identified could represent the first barrier for the detoxification and degradation of cyanide in the outermost layer of the tailings.

Correlation between the level of sulfane sulfur and the expression/activity of sulfurtransferases in chicken tissues – a possible ways of cyanide detoxification

Cyanogenic glycosides are a large group of secondary metabolites that are widely distributed in the many plants commonly consumed by humans, birds, and other animals. Thiosulfate sulfurtransferase (TST) and 3-mercaptopyruvate sulfurtransferase (MPST), are two evolutionary-related enzymes that constitute the defense against cyanide toxication and participate in the production of sulfane sulfur-containing compounds. The expression and activity of TST and MPST as well as the level of sulfane sulfur in chicken tissue homogenates of the liver, heart, and gizzard were investigated. The highest expression/activity of TST and MPST was noticed in liver homogenates which was associated with the high sulfane sulfur level. Both the expression and activity of TST as well as the sulfane sulfur level in chicken gizzard homogenates were significantly lower than in the liver and heart. Both TST and MPST enzymes can play an important role in cyanide detoxification in chicken tissues. Maintaining appropriate sulfane sulfur level together with the high activity of these enzymes is essential to protect tissues from the toxic effects of cyanide, released from certain nutrients.

The isolation of rumen enterococci strains along with high potential utilizing cyanide

Cyanogenic glycosides in forage species and the possibility of cyanide (CN) poisoning can have undesirable effects on ruminants. The literature estimates that unknown rumen bacteria with rhodanese activity are key factors in the animal detoxification of cyanogenic glycosides, as they are capable of transforming CN into the less toxic thiocyanate. Therefore, identifying these bacteria will enhance our understanding of how to improve animal health with this natural CN detoxification process. In this study, a rhodanese activity screening assay revealed 6 of 44 candidate rumen bacterial strains isolated from domestic buffalo, dairy cattle, and beef cattle, each with a different colony morphology. These strains were identified as belonging to the species Enterococcus faecium and E. gallinarum by 16S ribosomal DNA sequence analysis. A CN-thiocyanate transformation assay showed that the thiocyanate formation capacity of the strains after a 12 h incubation ranged from 4.42 to 25.49 mg hydrogen CN equivalent/L. In addition, thiocyanate degradation resulted in the production of ammonia nitrogen and acetic acid in different strains. This study showed that certain strains of enterococci substantially contribute to CN metabolism in ruminants. Our results may serve as a starting point for research aimed at improving ruminant production systems in relation to CN metabolism.

Quantitative Proteomic Analysis of Cyanide and Mercury Detoxification by Pseudomonas pseudoalcaligenes CECT 5344.

The cyanide-degrading bacterium Pseudomonas pseudoalcaligenes CECT 5344 uses cyanide and different metal-cyanide complexes as the sole nitrogen source. Under cyanotrophic conditions, this strain was able to grow with up to 100 μM mercury, which was accumulated intracellularly. A quantitative proteomic analysis by liquid chromatography-tandem mass spectrometry (LC-MS/MS) has been applied to unravel the molecular basis of the detoxification of both cyanide and mercury by the strain CECT 5344, highlighting the relevance of the cyanide-insensitive alternative oxidase CioAB and the nitrilase NitC in the tolerance and assimilation of cyanide, independently of the presence or absence of mercury. Proteins overrepresented in the presence of cyanide and mercury included mercury transporters, mercuric reductase MerA, transcriptional regulator MerD, arsenate reductase and arsenical resistance proteins, thioredoxin reductase, glutathione S-transferase, proteins related to aliphatic sulfonates metabolism and sulfate transport, hemin import transporter, and phosphate starvation induced protein PhoH, among others. A transcriptional study revealed that from the six putative merR genes present in the genome of the strain CECT 5344 that could be involved in the regulation of mercury resistance/detoxification, only the merR2 gene was significantly induced by mercury under cyanotrophic conditions. A bioinformatic analysis allowed the identification of putative MerR2 binding sites in the promoter regions of the regulatory genes merR5, merR6, arsR, and phoR, and also upstream from the structural genes encoding glutathione S-transferase (fosA and yghU), dithiol oxidoreductase (dsbA), metal resistance chaperone (cpxP), and amino acid/peptide extruder involved in quorum sensing (virD), among others. IMPORTANCE Cyanide, mercury, and arsenic are considered very toxic chemicals that are present in nature as cocontaminants in the liquid residues generated by different industrial activities like mining. Considering the huge amounts of toxic cyanide- and mercury-containing wastes generated at a large scale and the high biotechnological potential of P. pseudoalcaligenes CECT 5344 in the detoxification of cyanide present in these industrial wastes, in this work, proteomic, transcriptional, and bioinformatic approaches were used to characterize the molecular response of this bacterium to cyanide and mercury, highlighting the mechanisms involved in the simultaneous detoxification of both compounds. The results generated could be applied for developing bioremediation strategies to detoxify wastes cocontaminated with cyanide, mercury, and arsenic, such as those generated at a large scale in the mining industry.

Cyanide detoxification and iron mineral recycle of cyanide tailings by the sustainable utilization technology of oxidation-reduction roasting: Process optimization and mechanism study

The novel cyanide detoxification and resource utilization of cyanide tailings were treated sequentially by the oxidation-reduction roasting. Through a series of conditional experiments, the oxidation roasting realized the content of cyanide decrease to < 0.04 mg/kg (detection limit) with the removal rate reached to 99.99% at the optimum conditions. The reduction roasting realized the main mineral hematite transformed to magnetite and recycled the iron concentrate from the cyanide tailings with iron grade of 59.21% and iron recovery of 89.57%. The migration and transformation paths and decomposition products of cyanide during oxidative degradation process were investigated by the hexacyanoferrate reagents decomposition with the real-time concentration of CO2, XRD and FT-IR. The hexacyanoferrate decomposition reactions were complex, and divided into three stages, such as the room temperature-350 ℃, 350 ℃− 550 ℃, 550 ℃− 800 ℃ respectively. The transformation paths and decomposition products iron-cyanide complex were mainly as follows: K4Fe(CN)6 or K3Fe(CN)6 was oxidized and decomposed into CNO-, and further decomposed into CO3- by the roasting temperature increasing.

The role of cyanoalanine synthase and alternative oxidase in promoting salt stress tolerance in Arabidopsis thaliana

BackgroundCyanide is a toxic chemical that inhibits cellular respiration. In plants, cyanide can be produced by themselves, especially under stressful conditions. Cyanoalanine synthase (CAS) is a key enzyme involved in plant cyanide detoxification. There are three genes encoding CAS in Arabidopsis thaliana, but the roles of these genes in the plant’s response to stress are less studied. In addition, it is known that alternative oxidase (AOX) mediates cyanide-resistant respiration, but the relationship between CAS and AOX in regulating the plant stress response remains largely unknown.ResultsHere, the effects of the overexpression or mutation of these three CAS genes on salt stress tolerance were investigated. The results showed that under normal conditions, the overexpression or mutation of the CAS genes had no significant effect on the seed germination and growth of Arabidopsis thaliana compared with wild type (WT). However, under 50, 100, and 200 mM NaCl conditions, the seeds overexpressing CAS genes showed stronger salt stress resistance, i.e., higher germination speed than WT seeds, especially those that overexpressed the CYS-C1 and CYS-D1 genes. In contrast, the seeds with CAS gene mutations exhibited salt sensitivity, and their germination ability and growth were significantly damaged by 100 and 200 mM NaCl. Importantly, this difference in salt stress resistance became more pronounced in CAS-OE, WT, and mutant seeds with increasing salt concentration. The CAS-OE seeds maintained higher respiration rates than the WT and CAS mutant seeds under salt stress conditions. The cyanide contents in CAS mutant seeds were approximately 3 times higher than those in WT seeds and more than 5 times higher than those in CAS-OE seeds. In comparison, plants overexpressing CYS-C1 had the fastest detoxification of cyanide and the best salt tolerance, followed by those overexpressing CYS-D1 and CYS-D2. Furthermore, less hydrogen sulfide (H2S) was observed in CAS-OE seedlings than in WT seedlings under long-term salt stress conditions. Nonetheless, the lack of AOX impaired CAS-OE-mediated plant salt stress resistance, suggesting that CAS and AOX interact to improve salt tolerance is essential. The results also showed that CAS and AOX contributed to the reduction in oxidative damage by helping maintain relatively high levels of antioxidant enzyme activity.ConclusionIn summary, the findings of the present study suggest that overexpression of Arabidopsis CAS family genes plays a positive role in salt stress tolerance and highlights the contribution of AOX to CAS-mediated plant salt resistance, mainly by reducing cyanide and H2S toxicity.

Amperometric determination of salivary thiocyanate using electrochemically fabricated poly (3, 4-ethylenedioxythiophene)/MXene hybrid film

Thiocyanate (SCN) is a hazardous byproduct of the detoxification of cyanide. Even in minute quantity, the SCN has a negative impact on health. Although there are several ways for SCN analysis, an efficient electrochemical procedure has hardly ever been attempted. Here, the author reports the development of a highly selective and sensitive electrochemical sensor for SCN utilizing Poly (3, 4-Ethylenedioxythiophene) incorporated MXene (PEDOT/MXene) modified screen-printed electrode (SPE). The Raman, X-ray photoelectron (XPS), and X-ray diffraction (XRD) analyses support the effective integration of PEDOT on the MXene surface. Further, scanning electron microscopy (SEM) is employed to demonstrate the formation of MXene and PEDOT/MXene hybrid film. In order to specifically detect SCN in phosphate buffer media (pH 7.4), the PEDOT/MXene hybrid film is grown on the SPE surface via the electrochemical deposition method. Under the optimized condition, the PEDOT/MXene/SPE-based sensor provides a linear response against SCN from 10 to 100 µM and 0.1 μM to 1000 μM with the lowest limit of detections (LOD) of 1.44 μM and 0.0325 μM by differential pulse voltammetry (DPV) and amperometry, respectively. For accurate detection of SCN, our newly created PEDOT/MXene hybrid film-coated SPE demonstrates excellent sensitivity, selectivity, and repeatability. Ultimately, this novel sensor can be used to detect SCN precisely in environmental and biological samples.

Spatial-temporal variations of proline and related amino acids reveal distinct nitrogenous utilization strategies in rice during detoxification of exogenous cyanide

Cyanide (CN−) pollution in agricultural systems impairs amino acid metabolism in rice plants, hence decreasing their quality and yield. Meanwhile, little is known about the effects of CN− assimilation on the innate pool of proline (Pro) and its synthesis-related amino acids (Pro-AAs) in rice plants. In this study, a hydroponic experiment was carried out to investigate the effect of exogenous KCN on indigenous levels of Pro-AAs, i.e., Pro, glutamate (Glu), arginine (Arg), and ornithine (Orn) in rice seedlings fertilized with either nitrate (NO3−) or ammonium (NH4+) through the biochemical and RT-qPCR analysis. At the same KCN treatment concentration, the relative growth rate of NH4+-fed rice seedlings was considerably higher than that of NO3−-fed rice seedlings, but the residual concentration of CN− in NH4+-fed rice tissues was lower than that of NO3−-fed rice tissues. Based on the UPLC and stoichiometry molar ratio calculations, it is evident that the Glu pathway contributed significantly to Pro synthesis in rice under KCN + NO3− treatments; whereas the Orn pathway governed the synthesis of Pro in rice under KCN + NH4+ treatments. Moreover, transcriptional and bioinformatics analysis revealed that NH4+ fertilization resulted in spatial-temporal differences in the genetic response in rice tissue during detoxification of CN− compared with KCN + NO3− treatments. These findings suggested that the innate level of Pro serves as “a fishing float” to balance the flux between Pro and Pro-AAs in exogenous KCN-treated rice plants under different nitrogenous nutritional conditions.

Co-opted genes of algal origin protect C. elegans against cyanogenic toxins

Amygdalin is a cyanogenic glycoside enriched in the tissues of many edible plants, including seeds of stone fruits such as cherry (Prunus avium), peach (Prunus persica), and apple (Malus domestica). These plants biosynthesize amygdalin in defense against herbivore animals, as amygdalin generates poisonous cyanide upon plant tissue destruction.1,2,3,4 Poisonous to many animals, amygdalin-derived cyanide is detoxified by potent enzymes commonly found in bacteria and plants but not most animals.5 Here we show that the nematode C.elegans can detoxify amygdalin by a genetic pathway comprising cysl-1, egl-9, hif-1, and cysl-2. A screen of a natural product library for hypoxia-independent regulators of HIF-1 identifies amygdalin as a potent activator of cysl-2, a HIF-1 transcriptional target that encodes a cyanide detoxification enzyme in C.elegans. As a cysl-2 paralog similarly essential for amygdalin resistance, cysl-1 encodes a protein homologous to cysteine biosynthetic enzymes in bacteria and plants but functionally co-opted in C.elegans. We identify exclusively HIF-activating egl-9 mutations in a cysl-1 suppressor screen and show that cysl-1 confers amygdalin resistance by regulating HIF-1-dependent cysl-2 transcription to protect against amygdalin toxicity. Phylogenetic analysis indicates that cysl-1 and cysl-2 were likely acquired from green algae through horizontal gene transfer (HGT) and functionally co-opted in protection against amygdalin. Since acquisition, these two genes evolved division of labor in a cellular circuit to detect and detoxify cyanide. Thus, algae-to-nematode HGT and subsequent gene function co-option events may facilitate host survival and adaptation to adverse environmental stresses and biogenic toxins.

Comparative Transcriptomics and Methylomics Reveal Adaptive Responses of Digestive and Metabolic Genes to Dietary Shift in Giant and Red Pandas.

Both the giant panda (Ailuropoda melanoleuca) and red panda (Ailurus fulgens) belong to the order Carnivora, but have changed their dietary habits to eating bamboo exclusively. The convergent evolution characteristics of their morphology, genome and gut flora have been found in the two pandas. However, the research on the convergent adaptation of their digestion and metabolism to the bamboo diet, mediated by the dietary shift of the two pandas at the gene-expression and epigenetic regulation levels, is still lacking. We therefore used RNA sequencing among five species (two pandas and three non-herbivore mammals) and bisulfite sequencing among three species (two pandas and a carnivore ferret) to sequence key digestion and metabolism tissues (stomach and small intestine). Our results provide evidence that the convergent differentially expressed genes (related to carbohydrate utilization, bile secretion, Lys and Arg metabolism, vitamin B12 utilization and cyanide detoxification) of the two pandas are adaptive responses to the bamboo diet containing low lipids, low Lys and Arg, low vitamin B12 and high cyanide. We also profiled the genome-wide methylome maps of giant panda, red panda and ferret, and the results indicated that the promoter methylation of the two pandas may regulate digestive and metabolic genes to adapt to sudden environmental changes, and then, transmit genetic information to future generations to evolve into bamboo eaters. Taken together, our study provides new insights into the molecular mechanisms of the dietary shift and the adaptation to a strict bamboo diet in both pandas using comparative transcriptomics and methylomics.

Different regulation of auxin homeostasis would be a possible mechanism conferring quinclorac resistance in Echinochloa crusgalli var. zelayensis

AbstractDifferences in ethylene biosynthesis and cyanide detoxification have been reported to be mechanisms of quinclorac resistance in Echinochloa crusgalli var. zelayensis. Resistant phenotypes could be a consequence of the altered endogenous indole acetic acid (IAA) homeostasis induced by the herbicide. In this study, we determined the IAA content and expression levels of auxin homeostasis‐related genes in susceptible and resistant biotypes of E. crusgalli var. zelayensis after quinclorac treatment. The results showed that the IAA content of JNNX‐S (susceptible biotype) was significantly higher than that of SSXB‐R (resistant biotype) after treatment with 50 μM quinclorac. To better understand this rise in IAA, the expression profiles of seven genes (one for auxin synthesis, five for IAA conjugation and one for IAA oxidation) and the biochemical activities of two oxidases involved in IAA homeostasis were measured. The expression of EcYUCCA10 was significantly higher in JNNX‐S than in SSXB‐R. The expression levels of the EcGH3s were significantly lower in JNNX‐S than in SSXB‐R. These expression profiles were consistent with the elevation of IAA levels in the susceptible biotype. In contrast, EcUGT and EcDAO were induced in each biotype, but a smaller increase was observed in SSXB‐R than in JNNX‐S. The enzymatic activities of IAA oxidases and peroxidases were higher in SSXB‐R than in JNNX‐S 24 h after treatment. It was inferred that altered expression of specific genes involved in IAA synthesis, conjugation and oxidation resulted in less IAA being induced in the resistant biotype, resulting in a lower ethylene burst and the associated quinclorac resistance. These results suggest novel layers of complexity in the mechanism of quinclorac resistance.

Thiosulfate-Cyanide Sulfurtransferase a Mitochondrial Essential Enzyme: From Cell Metabolism to the Biotechnological Applications.

Thiosulfate: cyanide sulfurtransferase (TST), also named rhodanese, is an enzyme widely distributed in both prokaryotes and eukaryotes, where it plays a relevant role in mitochondrial function. TST enzyme is involved in several biochemical processes such as: cyanide detoxification, the transport of sulfur and selenium in biologically available forms, the restoration of iron–sulfur clusters, redox system maintenance and the mitochondrial import of 5S rRNA. Recently, the relevance of TST in metabolic diseases, such as diabetes, has been highlighted, opening the way for research on important aspects of sulfur metabolism in diabetes. This review underlines the structural and functional characteristics of TST, describing the physiological role and biomedical and biotechnological applications of this essential enzyme.

Thiosulfate sulfurtransferase prevents hyperglycemic damage to the zebrafish pronephros in an experimental model for diabetes

Thiosulfate sulfurtransferase (TST, EC 2.8.1.1), also known as Rhodanese, was initially discovered as a cyanide detoxification enzyme. However, it was recently also found to be a genetic predictor of resistance to obesity-related type 2 diabetes. Diabetes type 2 is characterized by progressive loss of adequate β-cell insulin secretion and onset of insulin resistance with increased insulin demand, which contributes to the development of hyperglycemia. Diabetic complications have been replicated in adult hyperglycemic zebrafish, including retinopathy, nephropathy, impaired wound healing, metabolic memory, and sensory axonal degeneration. Pancreatic and duodenal homeobox 1 (Pdx1) is a key component in pancreas development and mature beta cell function and survival. Pdx1 knockdown or knockout in zebrafish induces hyperglycemia and is accompanied by organ alterations similar to clinical diabetic retinopathy and diabetic nephropathy. Here we show that pdx1-knockdown zebrafish embryos and larvae survived after incubation with thiosulfate and no obvious morphological alterations were observed. Importantly, incubation with hTST and thiosulfate rescued the hyperglycemic phenotype in pdx1-knockdown zebrafish pronephros. Activation of the mitochondrial TST pathway might be a promising option for therapeutic intervention in diabetes and its organ complications.