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PubMed2002

Sorption and desorption of iron-cyanide complexes in deposited blast furnace sludge.

Blast furnace sludge is a waste originating from pig iron production and contains small amounts of iron-cyanide complexes. Leaching of iron-cyanide complexes from deposited blast furnace sludge into the ground water seems to be possible in principle. We investigated the sorption of the iron-cyanide complexes ferrocyanide, [FeII(CN)6](4-), and ferricyanide, [FeIII(CN)6](3-), in 22 samples of deposited blast furnace sludge in batch experiments. Subsequently, desorption of iron-cyanide complexes was investigated using 1 M NaCl. Sorption in five samples was evaluated with Langmuir isotherms. The blast furnace sludge samples were neutral to slightly alkaline (pH 7.6-9) and consisted of X-ray amorphous compounds and crystalline Fe oxides primarily. X-ray amorphous compounds are assumed to comprise coke-bound C and amorphous Fe, Zn, and Al oxides. The experiments that were evaluated with Langmuir isotherms indicated that the extent of ferricyanide sorption was higher than that of ferrocyanide sorption. Saturation of blast furnace sludge with iron-cyanide complexes was achieved. Sorption of iron-cyanide complexes in 22 blast furnace sludge samples at one initial concentration showed that 12 samples sorbed more ferrocyanide than ferricyanide. The extent of sorption largely differed between 0.07 and 2.76 Micromol [Fe(CN)6] m(-2) and was governed by coke-bound C. Ferricyanide sorption was negatively influenced by crystalline Fe oxides additionally. Only small amounts of iron-cyanide complexes sorbed in blast furnace sludge were desorbed by 1 M NaCl (ferrocyanide, 3.2%; ferricyanide, 1.1%, given as median). This indicated strong interactions of iron-cyanide complexes in blast furnace sludge. The mobility of iron-cyanide complexes in deposited blast furnace sludge and consequently contamination of the seepage and ground water was designated as low, because (i) deposited blast furnace sludge is able to sorb iron-cyanide complexes strongly, (ii) the solubility of the iron-cyanide-containing phase, K2Zn3[FeII(CN)6] . 9H20, is known to be low, and (iii) a worst case scenario of the transport of iron-cyanide complexes within the blast furnace sludge deposit indicated strong retardation of the complexes within the next 100 years.

Adsorption↗
PubMed2002

Exposure to cyanide following a meal of cassava food.

Exposure to cyanide from gari, a popular cassava food in West Africa, is implicated in the causation of ataxic polyneuropathy and amblyopia, but this has been questioned because cyanide was not detected in gari in a study. This study was carried out to determine if gari is a source of exposure to cyanide. Gari (150 g) containing cyanohydrin, from which 128 micromol of cyanide ions could be released, was dissolved in 500 ml of cold water for each of the 12 healthy subjects to drink. Concentrations of cyanide in plasma and erythrocytes were determined at baseline and following the meal at 30 min, 1 h, hourly for 4 h and two hourly for 12 h. The mean concentrations of cyanide in the plasma were 6 micromol/l (95% CI 2-10) at baseline, 12 micromol/l (95% CI 6-17) at peak and 6 micromol/l (95% CI 2-10) on return to baseline. The mean amount of cyanide absorbed into the plasma was 13 micromol (S.D. 12), while the transit time of absorbed cyanide was 7.3 h (S.D. 2.1). This study shows that exposure to cyanide follows consumption of gari, but the amount of cyanide absorbed into the plasma from a single meal is small and unlikely to cause acute intoxication. The long transit time of absorbed cyanide in the plasma suggests that frequent intake of gari could cause cyanide to accumulate in the plasma.

Adult↗
PubMed1995

Cyanide and carbon monoxide binding to the reduced form of cytochrome bo from Escherichia coli.

Cyanide binds to fully reduced cytochrome bo and induces a blue shift of the Soret absorption band of the high-spin heme o and a change in the visible region spectrum consistent with the expected conversion to a low-spin state. The dissociation constant, determined by titration of the extent of the binding spectrum, is 7.0 +/- 0.6 mM at pH 7.0. In contrast, cyanide does not bind significantly in this concentration range to the reduced form of cytochrome bd. The reduced cyanide compound of cytochrome bo can be laser photolyzed. Typically, less than 20% photolysis was attained with conditions that give essentially full photolysis of the carbon monoxide compound. The subsequent monophasic kinetics of recombination of cyanide at varying cyanide concentrations were used to determine kon, koff, and dissociation constant values at pH 7.0 of 572 +/- 43 M-1 s-1, 4.2 +/- 0.7 s-1, and 7.3 +/- 1.3 mM, respectively. The dissociation constant changes very little in the pH range 6-8, indicating that a proton is bound together with the cyanide anion, as predicted by our recent proposal of a requirement for electroneutrality in the binuclear center [Mitchell, R., & Rich, P. R. (1994) Biochim. Biophys. Acta 1186, 19-26]. Competition studies confirm that cyanide and carbon monoxide cannot bind simultaneously, so that their binding sites must overlap. A small fraction of the reduced unliganded enzyme appears to have a distinct photolysis spectrum in the absence of added ligands, and this is transformed into a typical ferrous cyanide compound only at very high cyanide concentrations. Cyanide binding and photolysis were also examined in a number of mutant forms of cytochrome bo, and in a wild-type form which was partially depleted in CuB. Dramatic changes in rate constants and binding constants were found in several cases. Data from several mutants were compared with analogous data on the binding and photolysis of carbon monoxide, and the effects of mutation were quite different with the two ligands. A model is developed to explain the observed effects of point mutations on the recombination kinetics of both carbon monoxide and cyanide. Overall, the results indicate that the CuB site is required for binding of cyanide, but not carbon monoxide, to the reduced enzyme, possibly by providing the site for binding of the associated proton.

Bacterial Proteins↗
PubMed2006

Cyanide metabolism of Pseudomonas pseudoalcaligenes CECT5344: role of siderophores.

Cyanide is one of the most potent and toxic chemicals produced by industry. The jewelry industry of Córdoba (Spain) generates a wastewater (residue) that contains free cyanide, as well as large amounts of cyano-metal complexes. Cyanide is highly toxic to living systems because it forms very stable complexes with transition metals that are essential for protein function. In spite of its extreme toxicity, some organisms have acquired mechanisms to avoid cyanide poisoning. The biological assimilation of cyanide needs the concurrence of three separate processes: (i) a cyanide-insensitive respiratory chain, (ii) a system for iron acquisition (siderophores) and (iii) a cyanide assimilation pathway. Siderophores are low-molecular-mass compounds (600-1500 Da) that scavenge iron (Fe(3+)) ions (usually with extremely high affinity) from the environment under iron-limiting conditions. There are two main classes of siderophores: catechol and hydroxamate types. The catechol-type siderophores chelate ferric ion via a hydroxy group, whereas the hydroxamate-type siderophores bind iron via a carbonyl group with the adjacent nitrogen. In the presence of cyanide, bacterial proliferation requires this specific metal uptake system because siderophores are able to break down cyano-metal complexes. Pseudomonas pseudoalcaligenes CECT5344 is able to use free cyanide or cyano-metal complexes as nitrogen source. A proteomic approach was used for the isolation and identification, in this strain, of a protein that was induced in the presence of cyanide, namely CN0, that is involved in siderophore biosynthesis in response to cyanide. An overview of bacterial cyanide degradation pathways and the involvement of siderophores in this process are presented.

Bacterial Proteins↗
PubMed1996

Protective effect of stroma-free methemoglobin during cyanide poisoning in dogs.

BACKGROUND: During fire exposure, cyanide toxicity can block aerobic metabolism. Oxygen and sodium thiosulfate are accepted therapy. However, nitrite-induced methemoglobinemia, which avidly binds cyanide, decreases oxygen-carrying capacity that is already reduced by the presence of carboxyhemoglobin (inhalation of carbon monoxide in smoke). This study tested whether exogenous stroma-free methemoglobin (SFmetHb) can prevent depression of hemodynamics and metabolism during canine cyanide poisoning. METHODS: In 10 dogs (weighing 18.8 +/- 3.5 kg) anesthetized with chloralose-urethane and mechanically ventilated with air, baseline hemodynamic and metabolic measurements were made. Then, 137 +/- 31 ml of 12 g% SFmetHb was infused into five dogs (SFmetHb group). Finally, the SFmetHb group and the control group (n = 5, no SFmetHb) received an intravenous potassium cyanide infusion (0.072 mg.kg-1.min-1) for 20 min. Oxygen consumption (VO2) was measured with a Datex Deltatrac (Datex Instruments, Helsinki, Finland) metabolic monitor and cardiac output (QT) was measured by pulmonary artery thermodilution. RESULTS: From baseline to cyanide infusion in the control group, QT decreased significantly (p < 0.05) from 2.9 +/- 0.8 to 1.5 +/- 0.4 l/min, mixed venous PCO2 (PvCO2) tended to decrease from 35 +/- 4 to 23 +/- 2 mmHg, PvO2 increased from 43 +/- 4 to 62 +/- 8 mmHg, VO2 decreased from 93 +/- 8 to 64 +/- 19 ml/min, and lactate increased from 2.3 +/- 0.5 to 7.1 +/- 0.7 mM. In the SFmetHb group, cyanide infusion did not significantly change these variables. From baseline to infused cyanide, the increases in blood cyanide (4.8 +/- 1.0 to 452 +/- 97 microM) and plasma thiocyanate cyanide (18 +/- 5 to 65 +/- 22 microM) in the SFmetHb group were significantly greater than those increases in the control group. SFmetHb itself caused no physiologic changes, except small decreases in heart rate and PvO2. Peak SFmetHb reached 7.7 +/- 1.0% of total hemoglobin. CONCLUSIONS: Prophylactic intravenous SFmetHb preserved cardiovascular and metabolic function in dogs exposed to significant intravenous cyanide. Blood concentrations of cyanide, and its metabolite, thiocyanate, revealed that SFmetHb trapped significant cyanide in blood before tissue penetration.

Animals↗
PubMed2004

Methods for assaying cyanide in bacterial culture supernatant.

AIMS: To find an easy, rapid and direct method for the quantitation of cyanide in a moderate number of bacterial culture supernatants. METHODS AND RESULTS: Culture supernatant from stationary phase cultures of Pseudomonas aeruginosa, grown in LB media, were analysed for cyanide content using the Merckoquant and Spectroquant cyanide detection kits as well as a cyanide ion-selective electrode (ISE) and a cyanide micro-ISE. The Merckoquant kit, designed for detection of low quantities of cyanide in water systems, proved not to be sufficiently reliable, providing poor comparison with previous assessments of cyanide levels in Ps. aeruginosa. The Spectroquant kit, and the two ISEs all provided very similar results, in agreement with previous data; however, it was the ISEs that fulfilled all the criteria for a rapid, direct test in a moderate number of samples. CONCLUSIONS: Cyanide ISEs can be used for easy assessment of the cyanide quantity in cultures grown in LB medium. SIGNIFICANCE AND IMPACT OF THE STUDY: The use of a cyanide ISE allows for an easy, direct and reproducible method for assaying cyanide in bacterial culture supernatant, which is of significant advantage over the currently accepted methods. This is especially important in an era of high-output genomic studies for assessing the phenotypic significance of data relating to the cyanide synthetic genes.

Culture Media↗
PubMed2001

Potential for error when assessing blood cyanide concentrations in fire victims.

The present study explores toxicologic significance of blood cyanide concentrations in fire victims. Headspace gas chromatography was used for cyanide detection. Analysis of blood samples from ten fire victims (postmortem interval = 8 h to 3 to 5 d) detected zero to 11.9 mg/L of cyanide and a large difference in cyanide concentrations among victims. Carboxyhemoglobin (COHb) saturation was in the range of 24.9 to 84.2%. To examine the effects of methemoglobinemia and postmortem interval on blood cyanide concentrations in fire victims, an experiment was carried out using rabbits as the animal model. The rabbits were sacrificed by intramuscular injection of 1 mL/kg 2% potassium cyanide 5 min after intravenous injection of 0.33 mL/kg of 3% sodium nitrite (Group A, n = 3) or physiological saline (Group B, n = 6). Average methemoglobin contents immediately before potassium cyanide administration were 6.9 and 0.8% in Groups A and B, respectively. Average cyanide concentrations in cardiac blood at the time of death were 47.4 and 3.56 mg/L, respectively. When blood-containing hearts of the rabbits (n = 3 for Group B) were left at 46 degrees C for the first 1 h, at 20 to 25 degrees C for the next 23 h and then at 4 degrees C for 48 h, approximately 85 and 46% of the original amounts of blood cyanide disappeared within 24 h in Groups A and B, respectively. After the 72-h storage period, 37 and 10%, respectively, of the original amounts of cyanide remained in the blood. When the other three hearts in Group B were left at 20 to 25 degrees C for the last 48 h without refrigeration, cyanide had disappeared almost completely by the end of the experiment. The present results and those published in the literature demonstrate that the toxic effects of cyanide on fire victims should not be evaluated based solely on the concentration in blood.

Animals↗
PubMed1986

Improved preparations of some per-O-acetylated aldohexopyranosyl cyanides.

3,4,6-Tri-O-acetyl-1,2-O-[1-(exo-, endo-cyano)ethylidene]-alpha-D- galacto- (1a/b), -alpha-D-gluco- (2a/b), and -beta-D-manno-pyranose (3a/b) were stereoselectively isomerized to the corresponding per-O-acetylated 1,2-trans-aldohexopyranosyl cyanides in 75, 16, and 62% yield, respectively, by treatment with boron trifluoride etherate in dry nitromethane. The corresponding per-O-acetylated 1,2-cis-aldohexopyranosyl cyanides were obtained concurrently in respective yields of 1.9, 0.9, and 4.8%. The per-O-acetylaldohexopyranosyl cyanide products were found stable to the reaction conditions and were readily isolated following completion of the rearrangement. It had previously been proved that reaction of 2,3,4,6-tetra-O-acetyl-alpha-D-manno- and -gluco-pyranosyl bromide with mercuric cyanide in nitromethane generates, in the ratio of approximately 1:1, the desired 1,2-trans-glycosyl cyanides and the corresponding 1,2-O-(1-cyanoethylidene) isomers (3a/b and 2a/b, respectively). Treatment of these reaction-mixtures with boron trifluoride etherate in nitromethane effected the rearrangement of 3a/b and 2a/b, thereby facilitating the isolation, and increasing the overall yields, of the per-O-acetylated 1,2-trans-D-manno- and -gluco-pyranosyl cyanides (58 and 30% total yield, respectively) relative to the earlier procedures. The boron trifluoride etherate-mediated reaction of per-O-acetyl-alpha- and -beta-D-galacto-, -alpha- and -beta-D-gluco-, -alpha-D-manno-, and -2-deoxy-2-phthalimido-beta-D-gluco-pyranoses with trimethylsilyl cyanide in nitromethane was also investigated. This reaction provides a "one-flask" synthesis of the corresponding per-O-acetylated 1,2-trans-aldohexopyranosyl cyanides in which 1,2-O-(1-cyanoethylidene) derivatives are isomerized in situ. Finally, improved preparations of the (not readily accessible) per-O-acetylated 1,2-cis-D-manno- and -gluco-pyranosyl cyanides are described. Thus, 2,3,4,6-tetra-O-acetyl-alpha- and -beta-D-mannopyranosyl cyanide (48 and 16% total yield, respectively) and -alpha- and -beta-D-glucopyranosyl cyanide (12 and 39% total yield, respectively) were synthesized by fusion of the corresponding alpha-D-glycosyl bromides with mercuric cyanide.

Carbohydrate Conformation↗
PubMed1984

Effect of cyanide on nitrovasodilator-induced relaxation, cyclic GMP accumulation and guanylate cyclase activation in rat aorta.

The effects of sodium cyanide on relaxation, increases in cyclic GMP accumulation and guanylate cyclase activation induced by sodium nitroprusside and other nitrovasodilators were examined in rat thoracic aorta. Cyanide abolished nitroprusside-induced relaxation and the associated increase in cyclic GMP levels. Basal levels of cyclic GMP and cyclic AMP were also depressed. Reversal of nitroprusside-induced relaxation by cyanide was independent of the tissue level of cyclic GMP prior to addition of cyanide. Incubation of nitroprusside with cyanide prior to addition to aortic strips did not alter the relaxant effect of nitroprusside. Sodium azide-, hydroxylamine-, N-methyl-N'-nitro-N-nitrosoguanide-, nitroglycerin- and acetylcholine-induced relaxations and increased levels of cyclic GMP were also inhibited by cyanide. Relaxations induced by nitric oxide were also inhibited by cyanide, although the relaxation with the low concentration of nitric oxide employed was not accompanied by detectable increases in cyclic GMP. Relaxation to 8-bromo-cyclic GMP was essentially unaltered by cyanide; however, isoproterenol-induced relaxation was inhibited. Guanylate cyclase in soluble and particulate fractions of aorta homogenates was activated by nitroprusside and the activation was prevented by cyanide. The present results suggest that cyanide inhibits nitrovasodilator-induced relaxation through inhibition of guanylate cyclase activation; however, cyanide may also have nonspecific effects which inhibit relaxation.

Animals↗
PubMed2000

A reproducible nonlethal animal model for studying cyanide poisoning.

Previous studies using bolus intravenous injections of sodium cyanide have been used to model the sudden exposure to high concentrations of cyanide that could occur on the battlefield. This study was designed to develop a model that would simulate the type of exposure to cyanide gas that could happen during actual low-level continuous types of exposure and then compare it with the bolus model. Cardiovascular and respiratory recordings taken from anesthetized dogs have been used previously to characterize the lethal effects of cyanide. The intravenous, bolus injection of 2.5 mg/kg sodium cyanide provides a model in which a greater than lethal concentration is attained. In contrast, our model uses a slow, intravenous infusion of cyanide to titrate each animal to its own inherent end point, which coincides with the amount of cyanide needed to induce death through respiratory arrest. In this model, therapeutic intervention can be used to restore respiration and allow for the complete recovery of the animals. After recovery, the same animal can be given a second infusion of cyanide, followed again by treatment and recovery, providing a reproducible end point. This end point can then be expressed as the total amount of cyanide per body weight (mg/kg) required to kill. In this study, the average dose of sodium cyanide among 12 animals was 1.21 mg/kg, which is approximately half the cyanide used in the bolus model. Thus, titration to respiratory arrest followed by resuscitation provides a repetitive-use animal model that can be used to test the efficacy of various forms of pretreatment and/or therapy without the loss of a single animal.

Acute Disease↗
PubMed1995

Cyanide inhibition of porcine kidney diamine oxidase and bovine plasma amine oxidase: evidence for multiple interaction sites.

The interactions of cyanide and phenylhydrazine with porcine kidney diamine oxidase (PKDAO) and bovine plasma amine oxidase (BPAO) (EC 1.4.3.6) have been investigated. Cyanide displays mixed noncompetitive inhibition against amine substrates and also against O2. EPR spectroscopy shows that cyanide binds to an equatorial site on Cu(II) and can be displaced by chloride, which is not an inhibitor, without recovery of activity, indicating that Cu(II)-bound cyanide is not inhibitory. 14CN-. studies have shown that one cyanide in PKDAO and two in BPAO are covalently and irreversibly bound per enzyme dimer at an unknown site, even under conditions where cyanide is not bound to Cu(II). These cyanides have no effect on activity or on binding of phenylhydrazine to the enzymes. Cyanide also binds reversibly to the organic cofactor in both enzymes, presumably as a cyanohydrin, leading to the observed mixed noncompetitive inhibition against substrate. In both enzymes, two phenylhydrazines react per enzyme dimer. The kinetics of phenylhydrazine titration are affected by cyanide, which indicates that phenylhydrazine and cyanide react at the same carbonyl group in the enzymes. The results suggest that inhibition of amine oxidases by cyanide is through a carbonyl reagent and a Cu(I) ligand rather than through a Cu(II) ligand.

Amine Oxidase (Copper-Containing)↗
PubMed1998

Degradation of cyanide in agroindustrial or industrial wastewater in an acidification reactor or in a single-step methane reactor by bacteria enriched from soil and peels of cassava.

During cassava starch production, large amounts of cyanoglycosides were released and hydrolysed by plant-borne enzymes, leading to cyanide concentrations in the wastewater as high as 200 mg/l. For anaerobic degradation of the cyanide during pre-acidification or single-step methane fermentation, anaerobic cultures were enriched from soil residues of cassava roots and sewage sludge. In a pre-acidification reactor this culture was able to remove up to 4 g potassium cyanide/l of wastewater at a hydraulic retention time (tHR) of 4 days, equivalent to a maximal cyanide space loading of 400 mg CN- 1(-1) day-1. The residual cyanide concentration was 0.2-0.5 mg/l. Concentrated cell suspensions of the mixed culture formed ammonia and formate in almost equimolar amounts from cyanide. Little formamide was generated by chemical decay. A concentration of up to 100 mmol ammonia/l had no inhibitory effect on cyanide degradation. The optimal pH for cyanide degradation was 6-7.5, the optimal temperature 25-37 degrees C. At a pH of 5 or lower, cyanide accumulated in the reactor and pre-acidification failed. The minimal tHR for continuous cyanide removal was 1.5 days. The enriched mixed culture was also able to degrade cyanide in purely mineralic wastewater from metal deburring, either in a pre-acidification reactor with a two-step process or in a one-step methanogenic reactor. It was necessary to supplement the wastewater with a carbon source (e.g. starch) to keep the population active enough to cope with any possible inhibiting effect of cyanide.

Aerobiosis↗
PubMed2006

The current and future applications of microorganism in the bioremediation of cyanide contamination.

Inorganic cyanide and nitrile compounds are distributed widely in the environment, chiefly as a result of anthropogenic activity but also through cyanide synthesis by a range of organisms including higher plants, fungi and bacteria. The major source of cyanide in soil and water is through the discharge of effluents containing a variety of inorganic cyanide and nitriles. Here the fate of cyanide compounds in soil and water is reviewed, identifying those factors that affect their persistence and which determine whether they are amenable to biological degradation. The exploitation of cyanides by a variety of taxa, as a mechanism to avoid predation or to inhibit competitors has led to the evolution in many organisms of enzymes that catalyse degradation of a range of cyanide compounds. Microorganisms expressing pathways involved in cyanide degradation are briefly reviewed and the current applications of bacteria and fungi in the biodegradation of cyanide contamination in the field are discussed. Finally, recent advances that offer an insight into the potential of microbial systems for the bioremediation of cyanide compounds under a range of environmental conditions are identified, and the future potential of these technologies for the treatment of cyanide pollution is discussed.

Bacteria↗
PubMed1985

Quantitative similarities in the several actions of cyanide on prostaglandin H synthase.

The effects of a heme ligand, cyanide, on pure ovine prostaglandin H synthase have been examined in detail as one approach to elucidating the role of the heme cofactor in cyclooxygenase and peroxidase catalysis by the synthase. Cyanide bound to the synthase heme with an affinity (Kd) of 0.19 mM, and inhibited the peroxidase activity of the synthase, with a KI value of 0.23 mM. Cyanide increased the sensitivity of the cyclooxygenase to inhibition by the peroxide scavenger, glutathione peroxidase. This increased sensitivity to inhibition reflected an increase in the level of peroxide required to activate the cyclooxygenase, from 21 nM in absence of cyanide to over 300 nM when 2.5 mM cyanide was present. The increase in peroxide activator requirement with increasing cyanide concentration closely paralleled the formation of the holoenzyme-cyanide complex. These effects of low levels of cyanide suggest that the heme prosthetic group of the synthase participates in the efficient activation of the cyclooxygenase by peroxide. Cyanide blocked the stimulation of cyclooxygenase velocity by phenol, but not the phenol-induced increase in overall oxygen consumption. This blockade by cyanide was noncompetitive with respect to phenol and was characterized by a KI of 4 mM. The higher KI value for this effect suggests that cyanide can also interact at a site other than the heme prosthetic group. The role of the heme prosthetic group in promoting efficient activation of the cyclooxygenase by peroxide appears to be central to the ability of the synthase to amplify the ambient peroxide concentration rapidly.

Animals↗
PubMed1993

Effects of cyanide on the striatal dopamine receptor binding in the rat.

In previous studies we have shown that sodium cyanide decreases the striatal dopamine levels within 60 s compared with the controls. Treatment with sodium cyanide also increases the naturally occurring 3,4-dihydroxy-L-phenylalanine (L-DOPA) in the striatum, but not in any other region studied. An increase in the in vivo synthesis of dopamine in cyanide-treated rats has also been observed. In order to further elucidate the effects on the central dopaminergic pathways the effects of sodium cyanide on the striatal dopamine D1 and dopamine D2 receptor binding were studied in vitro and after administration of sodium cyanide. In the rats injected with sodium cyanide (2.0 mg/kg, i.p.) the Bmax of the striatal dopamine D1 receptor binding was significantly decreased 15 min and 1 h after the treatment. The striatal dopamine D2 receptor binding was decreased only at 1 h after the cyanide administration. Neither sodium cyanide nor its metabolite sodium thiocyanate did significantly change the striatal dopamine D1 and D2 receptor binding in vitro. Accordingly sodium cyanide and sodium thiocyanate do not have direct effects on the dopamine receptors studied. The effects of cyanide on dopamine D1 and D2 receptors are probably in part due to the effect of cyanide on the release of dopamine.

Animals↗
PubMed2002

Antagonism of cyanide poisoning by dihydroxyacetone.

Dihydroxyacetone (DHA) effectively antagonized the lethal effect of cyanide in mice and rabbits, particularly if administered in combination with thiosulfate. Oral DHA (2 and 4 g/kg) given to mice 10 min before injection (i.p.) of cyanide increased the LD50 values of cyanide from 5.7 mg/kg to 12 and 17.6 mg/kg, respectively. DHA prevented cyanide-induced lethality most effectively, if given orally 10-15 min before injection of cyanide. A combination of pretreatment with oral DHA (4 g/kg) and post-treatment with sodium thiosulfate (1 g/kg) increased the LD50 of cyanide by a factor of 9.9. Furthermore, DHA given intravenously to rabbits 5 min after subcutaneous injection of cyanide increased the LD50 of cyanide from 6 mg/kg to more than 11 mg/kg, while thiosulfate (1 g/kg) given intravenously 5 min after cyanide injection increased the LD50 of cyanide only to 8.5 mg/kg. DHA also prevented the convulsions that occurred after cyanide intoxication.

Administration, Oral↗
PubMed2003

Chemical factors affecting the interpretation of blood cyanide concentrations in fire victims.

The purpose of this study was to examine the effects of methemoglobinemia caused by fire gases on blood cyanide concentrations in fire victims. Twenty-two fire victims with postmortem intervals of 8-48 h were involved. Blood cyanide concentrations at the time of death (C(0)) were estimated using the formula: C(0)=Ce(0.046 t) (C=blood cyanide concentration detected at autopsy, 0.046=first-order rate constant of cyanide disappearing from blood in corpses, and t=postmortem interval). Total (free and combined with cyanide) methemoglobin (MetHb) content was used to estimate the maximum capacity of MetHb for combining cyanide. Blood cyanide concentrations at the time of death were very high (5.32-6.47 mg/l) in five victims. Three showed high saturation (54.7-63.0%) of carboxyhemoglobin (CO-Hb) and elevated total MetHb contents (2.6-5.0%). MetHb at these levels is capable of scavenging up to 8.6-11.4 mg/l of blood cyanide. Thus, blood cyanide might have been completely combined with MetHb at the time of their death. In the remaining two victims, CO-Hb saturation was not high (30.9 and 37.9%) and no free MetHb was detected. As a result they may have exhibited severe toxic effects of cyanide at the time of their death. Our results indicate that MetHb contents and CO-Hb saturation should be determined to evaluate the toxic effects of cyanide in fire victims.

Adult↗
PubMed1989

Kinetics and mechanism of the reaction of cyanide with molybdenum nitrogenase from Azotobacter vinelandii.

The steady-state kinetic behavior of the six-electron reduction of N2 by nitrogenase is known to differ markedly from the six-electron reduction of cyanide in two ways. First, on extrapolation to infinite concentration of cyanide, the H2 evolution reaction is almost completely suppressed whereas at extrapolated infinite concentration of N2, H2 evolution continues. Second, as the ratio of the Fe protein to the MoFe protein increases, the reduction of N2 is favored over H2 evolution, whereas the reduction of cyanide becomes less favored relative to H2 evolution. We have extended these steady-state experiments with Azotobacter vinelandii nitrogenase to include a third observation, that the six-electron reduction of N2 is favored over H2 evolution at high total protein concentrations whereas cyanide reduction is less favored over H2 evolution at high total protein concentrations. All three steady-state observations can be explained by a model whereby cyanide is proposed to bind to a redox state of the MoFe protein more oxidized than that reactive toward H2 evolution and N2 reduction. To test this model, we have examined the pre-steady-state kinetic behavior of both cyanide reduction by A. vinelandii nitrogenase and cyanide inhibition of total electron flow through nitrogenase. The data show that in the presence or absence of cyanide there is a short lag of 100 ms before H2 is detected, followed by a linear phase of H2 evolution lasting for about 3 s, during which time no effects of cyanide are observable. After 3 s electron flow is finally inhibited by cyanide, and the cyanide reduction product CH4 is finally formed.(ABSTRACT TRUNCATED AT 250 WORDS)

Azotobacter↗