Formation Of Thiocyanate Research Articles

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.

Purification of highly concentrated cyanide-containing wastewater via stepwise recovering of valuable components

This study develops an efficient technique to purify the highly concentrated cyanide-containing industrial wastewater by recovering the valuable components. Firstly, sodium sulfide, sodium polysulfide and ferrous sulfate were respectively used as the precipitating agents to retrieve zinc, copper and iron from wastewater stepwise. In the meantime, cyanide presented as free cyanide and copper–cyanide complexes were transformed into thiocyanate by polysulfide. Afterwards, the solvent extraction of thiocyanate was systematically conducted with trioctylamine (TOA) as the extraction agent and sodium hydroxide solution as the stripping agent. The results showed that the contents of zinc, copper and iron in the solution after precipitation were less than 1 mg·L−1. Focusing on the reaction between copper–cyanide complex and polysulfide, three stages were established for the first time. In the first stage, Cu(CN)32− was gradually converted to CuCN0 and thiocyanate was rapidly generated. In the second stage, in addition to the formation of thiocyanate, Cu(I) was oxidized by polysulfide and precipitated as CuS ultimately. With an apparent activation energy of 70.9 kJ∙mol−1, kinetic analysis of the second stage suggested a significant effect of temperature on the copper–cyanide complex conversion rate. The apparent reaction orders of zero-valent sulfur and cyanide was 1.34 and 2.33, respectively. After the extraction and stripping process, the extraction efficiency of thiocyanate was nearly 100 % and the concentration of it can be enriched to 125 g·L−1 in the stripping solution. TOA and thiocyanic acid formed an extraction complex in a 1:1 ratio. This approach achieves the simultaneous recovery of valuable metallic ions (zinc, copper and iron) and cyanide conversion under the alkaline condition, which provides a new idea for the treatment of highly concentrated cyanide-containing wastewater with a complicated composition.

INCORPORATION OF SODIUM HYALURONATE AND NYAMPLUNG (Calophylum inophyllum) CAKE EXTRACT TO IMPROVE BIOPLASTIC CHARACTERISTIC

The cross-linking agent plays an important role in bioplastic mechanical properties. This study aimed to determine the effect of Sodium Hyaluronate (SoHA) as a synthetic cross-linking agent and the addition of Nyamplung Cake Extract (NCE) as an antimicrobial agent in the manufacture of bioplastic with hydroxypropyl starch (HPS) as based ingredient using the thermo-compression method. The novelty of the study was thiocyanate (SCN) formation in zone 3 (2161.66-2162.02/cm) and cyanate (C-N=O) in zone 6 (1,411.57 - 1,412.61/cm) of (1, 2 and 3%) SoHA bioplastic and cyanate formation in zone 6 and 7 (1,411.37 - 1,558.59/cm) of (1, 2 and 3%) SoHA – 20% NCE combined bioplastic originating from acetanilide group in SoHA and amide group in NCE. The formation of SCN and C-N=O in 2 and 3% SoHA bioplastic improved its sensitivity against gram-positive bacteria (Staphylococcus aureus) indicated by 0.6 mm and 0.45 mm inhibition zone, respectively. C-N=O formed in (1, 2 and 3%) SoHA – 20% NCE combined with bioplastic had 3.25 mm average inhibition zone against gram-positive bacteria (S. aureus), 2.75 mm against gram-negative bacteria (Escherichia coli), and 0.71 mm against fungi (Aspergillus niger). The analysis of mechanical properties showed that an addition of 3% SoHA was able to increase tensile strength and modulus of elasticity while reducing elongation, water solubility and water vapor permeability. Addition of (1, 2 and 3%) SoHA – 20% NCE resulted in a reverse effect. Keywords: acetanilide, amide, cross-linking agent, cyanate, thiocyanate

Sº and jarosite behavior during recovery of values from the direct leaching residue of sphalerite using cyanide and glycine

This paper reports the effect of the components of a direct leaching residue (jarosite and elemental sulfur), on the recovery of valuable metals such as gold and silver. Leaching media such as cyanide and mixtures of cyanide with glycine were used to recover the gold and silver from the residue; however, a low recovery of these metals was obtained. This occurred due to the negative effect of its components which caused problems in the extraction process such as encapsulation of silver (due to jarosite) and the formation of thiocyanate and re-precipitation of silver (due to sulfur). Various treatments prior to leaching were tested, finding that when the residue was desulfurized with perchlorethylene and subjected to an oxidizing alkaline hydrothermal treatment, the gold extraction increased from 39.73 to 88% and the silver extraction of 64.76 to 94.29%. Additionally, it was determined that when cyanide was assisted by glycine, the latter decreased the cyanide consumption by inhibition of the dissolution of iron and sulfur in cyanide.

Destabilisation of gold cyanide complex by sulphur species: A computational perspective

The interaction of gold cyanide complex with elemental sulphur and all metastable sulphur species has been studied using Density Functional Theory (DFT). The elemental sulphur and sulphide species formed during pre-treatment of refractory gold ores or dissolution of sulphide minerals form a series of metastable species including hydrosulphide, polysulphide, thionates, sulphite and finally sulphates which are known to have a detrimental effect on gold cyanidation. Previous researchers have attributed this effect mainly to passivation of the gold surface. However, interaction of dissolved aurocyanide with sulphur species has received almost no attention. Here, DFT molecular modelling has been used for the first time to describe the interaction of dissolved gold cyanide and sulphur species, and to explain the reduction and destabilisation potential of sulphur species in gold cyanidation.Computational modelling shows that sulphur species can have a significant negative effect on the stability of gold cyanide complex. Elemental sulphur and sulphide ion with −446.6 and − 198.4 kJ.mol−1 interaction energies have the most negative effect. S0 and S2− contribute to the destabilisation of gold cyanide via two different mechanisms of precipitation of AuCN and thiocyanate formation as well as reduction of gold by formation of sulphite and sulphates respectively. The effect of elemental sulphur can be neutralised by excess free cyanide in solution, while sulphide ion can still stay reactive toward gold cyanide in the presence of free cyanide. Addition of lead salt can decrease the inhibiting effect of sulphide ions by formation of lead sulphide. However, lead cannot eliminate the negative effect of elemental sulphur. It is concluded that oxidation of sulphur species can significantly overcome the adverse impact of sulphur species on the stability of gold cyanide complex. The destabilisation of gold cyanide complex by sulphur metastable species is introduced as one of the main mechanisms for loss of gold in sulphide gold ores.

Kinetics of Thiocyanate Formation by Reaction of Cyanide with Tetrathionate

In aquatic systems a reaction between tetrathionate and cyanide results in the formation of thiocyanate. We have studied kinetics of the reactions of tetrathionate with free cyanide and two cyanide complexes, hexacyanoferrate(II) and hexacyanoferrate(III), at the environmentally relevant conditions. For the reaction between tetrathionate and free cyanide, the rate constant and the activation energy, but not the reaction order, strongly depend on pH. Our observations allow to propose the following pathways of thiocyanate formation by the reactions of free cyanide with tetrathionate: (1) tetrathionate reacts relatively slow with hydrogen cyanide at acidic and neutral conditions; and (2) tetrathionate reacts relatively fast with cyanide anion under highly alkaline conditions. Depending on environmental conditions, the half-lives of the reaction between free cyanide and tetrathionate will be in the ranges of hours to several years. Reactions of tetrathionate with hexacyanoferrate(II) and hexacyanoferrate(III) have no environmental significance as they are slower than the decomposition of tetrathionate. Strategy for improvement of analytical protocols for analysis of tetrathionate and cyanide is proposed based on the detected kinetics parameters.

Reaction Chemistry of the syn-[Mo2O2(μ-S)2(S2)(DMF)3] Complex with Cyanide and Catalytic Thiocyanate Formation.

Removal of cyanide as nontoxic thiocyanate under physiological conditions may serve as a catalytic detoxification route in vivo. Aqueous catalytic reaction conditions were explored where at the conditions employed the reaction proceeded to exhaustion in 1 h. The complex, syn-[Mo2O2(μ-S)2(S2)(DMF)3] 1, participates in a ligand exchange reaction of the dimethylformamide ligands and cyanide. Simultaneous sulfur abstraction reaction from the terminal disulfide group forms thiocyanate and terminal sulfido ligand. Respective reaction rates for the two reactions appear competitive where different products were isolated solely based on change of reaction temperature. The approach to determine the number of cyanide ligands participating in the ligand exchange reaction by varying the stoichiometry and reaction temperature led to identification and isolation of tetranuclear complexes 2 and 5 and dinuclear complexes 3, 4, and 6. A synthesized and fully characterized thiocyanate analog of 6 (7) supports spectroscopic characterization of 6. The tetranuclear anion, [Mo4O4(μ-S)6(CN)4]4-, 2, was crystallized from a reaction at ambient temperature. The dinuclear anion, [Mo2O2(μ-S)2(S)(CN)3]3-, 3, was crystallized from similar reaction conditions at lower temperature. The reaction yield of thiocyanate obtained at pH of 7.4 and at 9.2 as a function of time, for several ratios of cyanide, favors the sulfur abstraction reaction at elevated pH. The sulfur abstraction reaction is the first step in a proposed mechanism of the reaction of cyanide and thiosulfate to form thiocyanate and sulfite by 1.

Organic thiocyanates - glucosinolate enzymatic degradation products or artefacts of the isolation procedure?

Glucosinolates are abundant in plants of the order Brassicales, and they are degraded by myrosinases into various organic breakdown products: isothiocyanates, thiocyanates, nitriles, etc., depending on their structure, conditions of hydrolysis, the presence of certain protein cofactors. Their most common hydrolysis products are isothiocyanates, while simple nitriles, epithionitriles, and thiocyanates are produced occasionally. Organic thiocyanates are described from a very limited number of Brassicales taxa. Up to now benzyl, (4-hydroxyphenyl)methyl, (4-methoxyphenyl)methyl, 4- methylthiobutyl, and allyl thiocyanates were reported as products of glucosinolates autolysis. The present review summarizes the knowledge on the mechanism of organic thiocyanate formation from the corresponding thioglucosides. The enzymatic formation of organic thiocyanates is believed to be enabled by thiocyanate-forming protein (TFP), but they could be formed via metabolic routes that do not involve TFP. All of the reported thiocyanates are produced from stable (carbo)cationic species that allow an isomerization of an isothiocyanate to thiocyanate, and vice versa. Although the possibility that thiocyanates can be biosynthesized in plats under certain conditions cannot be dismissed, allyl thiocyanate can be a thermal isomerization artefact of the original isothiocyanate that is formed in the heated zones of the gas chromatograph, while other thiocyanates could form in an aqueous medium via heterolytic dissociation to ambident nucleophilic SCN- and its recapture. One should always be aware of this analytical shortcoming when concluding on the presence and quantity of these specific (iso)thiocyanantes in the analyzed sample.

Gas chromatography-mass spectrometric identification of cyanide using a nucleophilic substitution based derivatization with S-phenyl benzenethiosulfonate.

A novel, simple and efficient analytical method for GC-MS based identification of cyanide has been developed using a single step nucleophilic substitution based derivatization of cyanide in aqueous medium. The nucleophilic substitution reaction of cyanide with S-phenyl benzenethiosulfonate results in the formation of phenyl thiocyanate as a cyanide derivative and it was found that the relative response of the resultant cyanide derivative was much higher than that of the cyanide derivatives resulting from disulfide based derivatizing agents. The sample preparation protocol for the identification of cyanide in aqueous samples was also optimized with the new derivatizing agent. Derivatization followed by liquid-liquid extraction was employed for the preparation of aqueous samples containing cyanide salts. The resultant samples were subjected to GC-MS analysis for the identification of the cyanide derivative. Under optimized conditions, the detection and quantification limits for cyanide aqueous samples were found to be 0.075 μg mL-1 and 0.25 μg mL-1 respectively. The calibration curve had a linear relationship with y = 0.086x - 0.076 and r2 = 0.997 for the working range of 0.25 μg mL-1 to 50 μg mL-1. The intraday RSDs were between 2.24 and 8.17%, and the interday RSDs were between 2.22 and 12.85%. The method can also be successfully employed for the identification of hydrogen cyanide in aqueous medium. The applicability of the present method was demonstrated by analysing a real sample from apple seed extraction.

Kinetics of Thiocyanate Formation by Reaction of Cyanide and Its Iron Complexes with Thiosulfate

Reactions between cyanide and compounds, which contain S–S bonds, in aqueous media result in formation of thiocyanate. In this work, we studied the kinetics of reactions of thiosulfate with free cyanide and its complexes under environmental conditions. Rates of reactions between cyanide species and thiosulfate decrease in the following order: CN− > HCN > [Fe(CN)6]3− > [Fe(CN)6]4−. However, at neutral and slightly acidic pH range, reaction of thiosulfate with iron-cyanide complexes outcompetes its reaction with free cyanide, which exists in equilibrium with complexed cyanide. At environmentally relevant conditions, the characteristic time of reaction between free cyanide and thiosulfate was found to be tens of thousands of years, while for iron-cyanide complexes it was found to be hundreds to millions of years. Examples of application of kinetic parameters for calculation of rates of cyanide consumption in industrial (coke oven wastewater) and non-polluted natural aquatic system (Delaware Great Marsh) are provided.

Iron is a centrally bound cofactor of specifier proteins involved in glucosinolate breakdown.

Glucosinolates, a group of sulfur-rich thioglucosides found in plants of the order Brassicales, have attracted a lot of interest as chemical defenses of plants and health promoting substances in human diet. They are accumulated separately from their hydrolyzing enzymes, myrosinases, within the intact plant, but undergo myrosinase-catalyzed hydrolysis upon tissue disruption. This results in various biologically active products, e.g. isothiocyanates, simple nitriles, epithionitriles, and organic thiocyanates. While formation of isothiocyanates proceeds by a spontaneous rearrangement of the glucosinolate aglucone, aglucone conversion to the other products involves specifier proteins under physiological conditions. Specifier proteins appear to act with high specificity, but their exact roles and the structural bases of their specificity are presently unknown. Previous research identified the motif EXXXDXXXH as potential iron binding site required for activity, but crystal structures of recombinant specifier proteins lacked the iron cofactor. Here, we provide experimental evidence for the presence of iron (most likely Fe2+) in purified recombinant thiocyanate-forming protein from Thlaspi arvense (TaTFP) using a Ferene S-based photometric assay as well as Inductively Coupled Plasma-Mass Spectrometry. Iron binding and activity depend on E266, D270, and H274 suggesting a direct interaction of Fe2+ with these residues. Furthermore, we demonstrate presence of iron in epithiospecifier protein and nitrile-specifier protein 3 from Arabidopsis thaliana (AtESP and AtNSP3). We also present a homology model of AtNSP3. In agreement with this model, iron binding and activity of AtNSP3 depend on E386, D390, and H394. The homology model further suggests that the active site of AtNSP3 imposes fewer restrictions to the glucosinolate aglucone conformation than that of TaTFP and AtESP due to its larger size. This may explain why AtNSP3 does not support epithionitrile or thiocyanate formation, which likely requires exact positioning of the aglucone thiolate relative to the side chain.

Study of the Structure of Lithium Thiocyanate Complexes with Benzo-15-Crown-5 by X-ray Diffraction and IR Spectroscopy

The complex formation of lithium thiocyanate with benzo-15-crown-5 (B15C5) was studied. The possibility of formation of both anhydrous and crystal water-containing complexes was demonstrated. The complexes LiB15C5NCS and LiB15C5H2ONCS were synthesized and characterized by X-ray diffraction and IR spectroscopy.

Crystal Growth and Structural Characterization of a Thiocyanato-Bridged Copper(I/II) Mixed-Valence Coordination Polymer

A new mixed-valence coordination polymer [Cu3(SCN)4(DMSO)2] n (SCN– = thiocyanato and DMSO = dimethyl sulfoxide) was prepared and characterized by single crystal X-ray diffraction method. The in situ formation of thiocyanate during the synthesis induces reduction of a part of Cu(II) to Cu(I). The three-dimensional structure of the binuclear thiocyanato bridged compound provided an example of pseudohalide materials containing two different environments for both copper centers.

A single-domain rhodanese homologue MnRDH1 helps to maintain redox balance in Macrobrachium nipponense

Rhodaneses are known to catalyze in vitro the transfer of a sulfane sulfur atom from thiosulfate to cyanide with concomitant formation of thiocyanate, however, their biological functions remain speculative despite the main role is considered as detoxifying cyanide especially in animal livers. In this study, we characterized a single-domain rhodanese homologue, MnRDH1, from Macrobrachium nipponense. We found MnRDH1 with the highest expression in hemocytes. Upon Aeromonas hydrophila challenge, expression of MnRDH1 was up-regulated in various tissues, including hepatopancreas, gill, intestine and hemocytes. RNAi knockdown of MnRDH1 led to rapid increases of malondialdehyde content, which reveals that MnRDH1 deficiency causes oxidative stress. The expression of MnRDH1 in hepatopancreas was significantly increased in response to the doxorubicin-induced oxidative stress, indicating the gene is oxidative stress inducible. We transformed E. coli with MnRDH1 and the mutant MnRDH1C75A, and found significant rhodanese activity of the recombinant protein of MnRDH1 in vitro, but detected no enzyme activity of the mutant MnRDH1C75A. When under the oxidative insult by H2O2, the MnRDH1 transformed E. coli had significantly enhanced survival rates compared to those bacteria transformed with MnRDH1C75A. In conclusion, our study demonstrates that rhodanese in M. nipponense confers oxidative stress tolerance, and thus renders an evidence for the notion that rhodanese family genes act a critical role in antioxidant defenses.

Improvements in gold ore cyanidation by pre-oxidation with hydrogen peroxide

It is known that the presence of sulphidic minerals in the cyanidation of gold ores may cause significant consumption of oxygen supplied in the injected air. This may result in dissolved oxygen starvation for the oxidative leaching of the gold, and ultimately it will reduce the maximum attainable recovery of gold from the ore. In addition, the presence of sulphides leads to extra consumption of the cyanide-leaching agent, NaCN, due to the formation of thiocyanate, therefore increasing costs. These types of gold sulphidic ores may be pre-treated prior to cyanidation by means of an oxidation step, converting the sulphides into oxides or sulphates. This treatment leads to a reduction in the consumption of dissolved oxygen and of cyanide in the cyanidation step and to an improvement in the metallurgical recovery. In the current work we present the results of a five month full-scale trial carried out in a gold extraction plant in Brazil, which normally operated with three tanks in series carrying out an alkaline pre-oxidation step using compressed air only, followed by a train of fourteen aerated and mechanically-agitated tanks for the cyanidation. The ore feeding the leaching circuit averages 1.70gAu/t, with about 2.5% of pyrrhotite (FeS) as the main sulphide constituent. The addition of 60L/h of concentrated hydrogen peroxide, H2O2, 50%w/w (density=1.19g/mL) for pre-oxidation of a slurry of 60% solids at a rate of 150t/h (dry ore) resulted in a marked increase in dissolved oxygen (DO). This addition corresponds to a dosing rate of 0.24kg 100%H2O2 per ton of dry ore and increased the dissolved oxygen level from an average of about 1.0 to 7.2mg/L in the pre-oxidation tanks. It also led to an overall reduction of NaCN consumption from an average of 0.52 to 0.40kg/t of ore, and an increase in metallurgical Au recovery from an average of 91.3% to 92.5%.

Degradation of thiocyanate in aqueous solution by persulfate activated ferric ion

Thiocyanate formation from cyanidation of gold bearing ores is becoming a more common problem during gold processing. In this work, the application of an advanced oxidation process based on the use of persulfate (S2O82−) as an environmentally friendly oxidant in the presence of ferric ion for destruction of a persistent and non-volatile inorganic contaminant, such as thiocyanate, in aqueous solutions is reported for the first time. The influence of various reaction parameters like ferric ion and persulfate dosage, initial thiocyanate concentration and the influence of radical scavenger are examined. An accelerated reaction using S2O82− to destroy thiocyanate can be achieved via chemical activation with Fe3+ to generate highly reactive sulfate anion-radicals (SO4−). The results showed that degradation efficiency was negligible when persulfate was used alone, ferric ions significantly improved the degradation efficiency of thiocyanate at ambient temperature. Under the optimum molar ratios ([S2O82−]:[SCN−]=5:1 and [S2O82−]:[Fe3+]=1:0.2), 99% of thiocyanate present in aqueous solution at the initial concentration range of 1.72–17.2mM was degraded within 60min of reaction time. To evaluate the contribution of reactive free radicals generated through Fe(III)-mediated activation of persulfate to thiocyanate degradation, quenching experiments using methanol as the radical quenching agent were carried out. The obvious decrease in thiocyanate oxidation efficiency in the presence of methanol confirmed that the radical-based pathway was the dominant mechanism in Fe3+/S2O82− system. The degradation of thiocyanate was accompanied by the formation of cyanide as the main final product of the reaction. Thus the catalytic oxidation of thiocyanate makes it possible to return NaCN into the production process for leaching of precious metals. The work presents an efficient and environmentally acceptable wastewater treatment process applicable in mining facilities utilizing cyanidation of sulfide ores and/or concentrates.

ChemInform Abstract: General and Practical Formation of Thiocyanates from Thiols.

AbstractA new method for the cyanation of thiols (I), (VI), and disulfides (IX) using cyanobenziodoxol(on)e hypervalent iodine reagents, such as (II) and (VII) is described.

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

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.

General and practical formation of thiocyanates from thiols.

A new method for the cyanation of thiols and disulfides using cyanobenziodoxol(on)e hypervalent iodine reagents is described. Both aliphatic and aromatic thiocyanates can be accessed in good yields in a few minutes at room temperature starting from a broad range of thiols with high chemioselectivity. The complete conversion of disulfides to thiocyanates was also possible. Preliminary computational studies indicated a low energy concerted transition state for the cyanation of the thiolate anion or radical. The developed thiocyanate synthesis has broad potential for various applications in synthetic chemistry, chemical biology and materials science.

Antidotes of cyanide intoxication

Cyanide poisoning can occur from industrial disasters, smoke inhalation from fire, food, and multiple other sources. Cyanide inhibits mitochondrial oxidative phosphorylation by blocking mitochondrial cytochrome oxidase, which in turn results in anaerobic metabolism and depletion of adenosine triphosphate in cells. Rapid administration of antidote is crucial for life saving in severe cyanide poisoning. Multiple antidotes are available for cyanide poisoning. The action mechanism of cyanide antidotes include formation of methemoglobin, production of less or no toxic complex, and sulfane sulfur supplementation. At present, the available antidotes are amyl nitrite, sodium nitrite, sodium thiosulfate, hydroxocobalamin, 4-dimethylaminophenol, and dicobalt edetate. Amyl nitrite, sodium nitrite, and 4-dimethylaminophenol induce the formation of methemoglobin. Sodium thiosulfate supplies the sulfane sulfur molecule to rhodanese, allowing formation of thiocyanate and regeneration of native enzymes. Hydroxocobalamin binds cyanide rapidly and irreversibly to form cyanocobalamin. Dicobalt edetate acts as a chelator of cyanide, forming a stable complex. Based on the best evidence available, a treatment regimen of 100% oxygen and hydroxocobalamin, with or without sodium thiosulfate, is recommended for cyanide poisoning. Amyl nitrite and sodium nitrite, which induce methemoglobin, should be avoided in victims of smoke inhalation because of serious adverse effects.