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PubMed1992

Carbamylation and glycosylation of haemoglobin in vitro: effects of cyanate and glucose.

An in vitro system that is independent of any haemodynamic influence and other physiological controls was designed to study the formation of carbamylated and glycosylated haemoglobin, by the use of cyanate and glucose respectively, incubated with whole-blood from normal healthy subjects. In this system the formation of glycosylated haemoglobin is more favourable than that of carbamylated haemoglobin. The effect of glucose in reducing the formation of carbamylated haemoglobin is greater than the effect of cyanate on the formation of glycoslyated haemoglobin. There is a strong correlation coefficient (r = 0.9, P < 0.005) for the relationship between the formation of carbamylated and glycosylated haemoglobin in this system.

Cyanates↗
PubMed1975

Tumor-selective inhibition of the incorporation of 3H-labeled amino acids into protein by cyanate.

Sodium cyanate at a dose level of 125 or 250 mg/kg i.p. caused an inhibition of incorporation of 3H-labeled amino acids into cytoplasmic and nuclear proteins of the rapidly growing hepatoma 7777 and the slowly growing hepatoma 9618A. There was no inhibitory effect on 3H-labeled amino acid incorporation into protein in the livers of rats bearing these tumors. Studies on the effects of sodium cyanate on incorporation of 3H-labeled amino acids into total acid-insoluble material indicated that a greater than 85% inhibition could be achieved in hepatoma 5123C, hepatoma 9618A2, and the MK3 kidney tumor with either little or no effect in host liver, kidneys, brain, skeletal muscle, intestinal mucosa, and regenerating liver after partial hepatectomy.

Amino Acids↗
PubMedDate not supplied

An ultrastructural study of chronic sodium cyanate-indiuced neuropathy.

Fifteen rats were given a sodium cyanate-rich diet for 18 months and at the end of that period, all of them had developed motor weakness and were perfused for ultrastructural study. A peripheral neuropathy involving mostly the roots and sciatic nerves was found and the main ultrastructural lesion was vacuolization of myelin. There was marked distinction of the myelin sheaths and phagocytosis of myelin. Axoplasmic changes were minimal and consisted of accumulation of glycogen within vacuoles. Invaginations of adaxonal Schwann cell membranes and axolemma forming loops and separate chambers were also present. There was active participation of macrophages in the splitting of myelin as well as in phagocytosis of myelin remnants. There was evidence of remyelination with the toxic damage. We concluded that cyanate induced neuropathy is due mostly to a myelinotoxic effect of the drug, although parallel but less intense axonal damage cannot be excluded.

Animals↗
PubMedDate not supplied

[Potassium cyanate modification of the toxic and mutagenic effects of gamma radiation and benzo(a)pyrene].

In experiments with CHO-AT3-2 cell culture, a study was made of the effect of potassium cyanate (KNCO) on the effect of gamma radiation and benzo(a)pyrene (BP) by the following tests: cell viability, induction of cells with micronuclei and fragmented nuclei and mutations by thymidine kinase (TK) and Na+/K+-ATPase loci. Some tests have revealed the increase in the effect of gamma radiation and BP produced by potassium cyanate. It is suggested that the sensitizing effects are related to repair system inhibition and/or changes in the cell chromatin structure produced by KNCO.

Animals↗
PubMed1979

Effects of cyanate, thiocyanate, and amygdalin on metabolite uptake in normal and neoplastic tissues of the rat.

Thiocyanate was found to resemble cyanate in its inhibitory effects on [3H]thymidine incorporation and the uptake of [32P]phosphate and [3H]amino acids in transplanted tumors of the BUF rat. The capacity to inhibit metabolite uptake in hepatomas and a colon tumor under conditions in which uptake was unchanged or increased in host liver was concluded to be a common feature of the action of cyanate and thiocyanate. Inhibition of [32P]phosphate uptake and [3H]thymidine incorporation into DNA of tumors was also observed after treatment of rats with amygdalin. With this drug, however, the action on tumors and livers of host rats was similar.

Amino Acids↗
PubMed1981

Inhibition of carcinogen-induced neoplasia by sodium cyanate, tert-butyl isocyanate, and benzyl isothiocyanate administered subsequent to carcinogen exposure.

The effects of sodium cyanate, tert-butyl isocyanate, and benzyl isothiocyanate on carcinogen-induced neoplasia were studied in experiments in which the test compound was fed starting 1 week following completion of carcinogen administrations. Under these conditions, all three test compounds exerted an inhibitory effect on the occurrence of 7,12-dimethylbenz(a)anthracene-induced neoplasia of the breast of Sprague-Dawley rats. In a second experiment model, sodium cyanate inhibited the occurrence of 1,2-dimethylhydrazine-induced neoplasia of the large bowel of female CF-1 mice. Thus, a new group of compounds has been identified which has inhibitory capacities against neoplasia when given subsequent to carcinogen exposure.

9,10-Dimethyl-1,2-benzanthracene↗
PubMed1982

Clinical studies of a continuous extracorporeal cyanate treatment system for patients with sickle cell disease.

An extracorporeal carbamylation system was evaluated in two patients with sickle cell disease. Access was achieved with existing veins in one patient and an AV fistula in the second. Modifications in the treatment procedure were made as experience indicated. Levels of carbamylation of greater than 1 mol/mol of hemoglobin tetramer were achieved with 4 to 6 hr of treatment every 2 weeks. Cyanate returned to the patient averaged 68.5 mg per treatment. As expected, P50 values decreased and hemoglobin levels increased as the treatment progressed. Patterns of cyanate distribution among the red cell population were those predicted by computer calculations. These observations document the safety and reliability of the treatment system but do not permit conclusions as to efficacy.

Adult↗
PubMed2002

The di-iron subsite of all-iron hydrogenase: mechanism of cyanation of a synthetic [2Fe3S]-carbonyl assembly.

This paper describes the kinetics and intimate mechanisms associated with cyanation of [2Fe3S] assemblies to give species structurally related to the subsite of all-iron hydrogenase. Stopped-flow FTIR spectroscopy has enabled the quantitation of the dynamics of five well-defined steps that experimentally illustrate the role of bridging carbonyls in the assembly of the dicyanide species, how on-off sulfur ligation can have a dramatic effect on cyanation kinetics and how the [2Fe3S] core stabilises bridging carbonyl species.

Carbon Monoxide↗
PubMed2005

Dissecting the intimate mechanism of cyanation of {2Fe3S} complexes related to the active site of all-iron hydrogenases by DFT analysis of energetics, transition states, intermediates and products in the carbonyl substitution pathway.

A bridging carbonyl intermediate with key structural elements of the diiron sub-site of all-iron hydrogenase has been experimentally observed in the CN/CO substitution pathway of the {2Fe3S} carbonyl precursor, [Fe(2)(CO)(5){MeSCH(2)C(Me)(CH(2)S)(2)}]. Herein we have used density functional theory (DFT) to dissect the overall substitution pathway in terms of the energetics and the structures of transition states, intermediates and products. We show that the formation of bridging CO transitions states is explicitly involved in the intimate mechanism of dicyanation. The enhanced rate of monocyanation of {2Fe3S} over the {2Fe2S} species [Fe(2)(CO)(6){CH(2)(CH(2)S)(2)}] is found to rest with the ability of the thioether ligand to both stabilise a mu-CO transition state and act as a good leaving group. In contrast, the second cyanation step of the {2Fe3S} species is kinetically slower than for the {2Fe2S} monocyanide because the Fe2 atom is deactivated by coordination of the electron-donating thioether group. In addition, hindered rotation and the reaction coordinate of the approaching CN(-) group, are other factors which explain reactivity differences in {2Fe2S} and {2Fe3S} systems. The intermediate species formed in the second cyanation step of {2Fe3S} species is a mu-CO species, confirming the structural assignment made on the basis of FT-IR data (S. J. George, Z. Cui, M. Razavet, C. J. Pickett, Chem. Eur. J. 2002, 8, 4037-4046). In support of this we find that computed and experimental IR frequencies of structurally characterised {2Fe3S} species and those of the bridging carbonyl intermediate are in excellent agreement. In a wider context, the study may provide some insight into the reactivity of dinuclear systems in which neighbouring group on-off coordination plays a role in substitution pathways.

Binding Sites↗
PubMed2007

Palladium-catalyzed enantioselective domino heck-cyanation sequence: development and application to the total synthesis of esermethole and physostigmine.

An efficient synthesis of functionalized 3-alkyl-3-cyanomethyl-2-oxindole 1 by a palladium-catalyzed domino Heck-cyanation reaction has been developed. Reaction of ortho-iodoanilide 5 with potassium ferro(II)cyanide, K(4)[Fe(CN)(6)], dissolved in DMF in the presence of palladium acetate and sodium carbonate afforded oxindole 1 in good to excellent yields. An enantioselective domino Heck-cyanation process has been developed for the first time using (S)-DIFLUORPHOS as a chiral supporting ligand, and an enantioselectivity of up to 79 % ee in the enantiomerically enriched oxindole was obtained under optimized conditions. A concise total synthesis of esermethole and physostigmine, powerful inhibitors of acetyl- and butyryl-cholinesterase, is documented.

Catalysis↗
PubMed2004

Crystal structure and magnetic interactions in nickel(II) dibridged complexes formed by two azide groups or by both phenolate oxygen-azide, -thiocyanate, -carboxylate, or -cyanate groups.

Tridentate/tetradentate Schiff base ligands L(1) and L(2), derived from the condensation of o-vanillin or pyridine-2-aldehyde with N,N-dimethylethylenediammine, react with nickel acetate or perchlorate salt and azide, cyanate, or thiocyanate to give rise to a series of dinuclear complexes of formulas [Ni(L(1))(micro(1,1)-N(3))Ni(L(1))(N(3))(OH(2))].H(2)O (1), [[Ni(L(1))(micro(1,1)-NCS)Ni(L(1))(NCS)(OH(2))][Ni(L(1))(micro-CH(3)COO)Ni(L(1))( NCS) (OH(2))]] (2) [[2A][2B]], [Ni(L(1))(micro(1,1)-NCO)Ni(L(1))(NCO)(OH(2))].H(2)O (3), and [Ni(L(2)-OMe)(micro(1,1)-N(3))(N(3))](2) (4), where L(1) = Me(2)N(CH(2))(2)NCHC(6)H(3)(O(-))(OCH(3)) and L(2) = Me(2)N(CH(2))(2)NCHC(6)H(3)N. We have characterized these complexes by analytical, spectroscopic, and variable-temperature magnetic susceptibility measurements. The coordination geometry around all of the Ni(II) centers is a distorted octahedron with bridging azide, thiocyanate/acetate, or cyanate in a micro(1,1) mode and micro(2)-phenolate oxygen ion for 1-3, respectively, or with a double-bridging azide for 4. The magnetic properties of the complexes were studied by magnetic susceptibility (chi(M)) versus temperature measurements. The chi(M) nus T plot reveals that compounds 1 and 4 are strongly ferromagnetically coupled, 3 shows a weak ferromagnetic behavior, and 2 is very weakly antiferromagnetically coupled.

Journal Article↗
PubMed2003

Copper-catalyzed domino halide exchange-cyanation of aryl bromides.

An efficient copper-catalyzed domino halogen exchange-cyanation procedure for aryl bromides was developed utilizing 10 mol % CuI, 20 mol % KI, 1.0 equiv of the inexpensive N,N'-dimethylethylenediamine as ligand, and 1.2 equiv of NaCN in toluene at 110 degrees C. The new method represents a significant improvement over the traditional Rosenmund-von Braun reaction: the reaction conditions are much milder, and the use of stoichiometric amounts of copper(I) cyanide and polar solvents is avoided; therefore the isolation and purification of the aromatic nitrile products is greatly simplified. In addition, the new method exhibits excellent functional group compatibility comparable to that of the analogous Pd-catalyzed cyanation methodology.

Catalysis↗
PubMed1999

Theoretical Study on the Mechanism of Formation of Cyanate Resins.

Ab initio calculations of a formation reaction of a triazine ring were performed. From the model substrate, methyl cyanate, a concerted association path with C(3)(h)() symmetry was first examined. In terms of energy changes, this path was found to be unlikely. Second, a stepwise path assisted by a water cluster was tested. But, this path was found to be of a relatively high amount of activation energy in the first additional step. Third, a zinc formate was used as a catalyst, and the reaction was computed to have a reasonable stepwise route for formation of the six-membered triazine ring. Fourth, the reaction promoted by a hydronium ion was shown to generate a ring-closure mechanism similar to that caused by the zinc catalyst. Thus, the crucial role of catalysts coordinated to the sigma lone-pair orbital of the cyanate nitrogen atom was verified.

Journal Article↗
PubMed2004

Palladium-catalyzed cyanation of aryl bromides promoted by low-level organotin compounds.

A novel method for palladium-catalyzed cyanation of aryl bromides promoted by low-level tri-n-butyltin chloride or cyanide is described. The method features low catalyst loading and mild reaction conditions. KCN is used as the cyanide source. Only trace levels of the tri-n-butyltin compound are required to achieve high conversion and yield in the cyanation of aryl bromides, iodides, and triflates.

Journal Article↗
PubMed1997

Is cyanate a carbonic anhydrase substrate?

A study was undertaken to investigate whether diverse carbonic anhydrase (CA) isozymes (both native Zn as well as cobalt-substituted) are able to catalyze the hydrolysis of anions such as cyanide, cyanate, and thiocyanate. A controversy exists between the crystallographic and spectroscopic data of CA II-anion adducts. In the former case it has been shown that "metal poisons" such as CN- and CNO- are not directly coordinated to the active site Zn(II) ion whereas spectroscopic studies indicate otherwise. A theoretical study in the above systems did not resolve this controversy, since it was calculated that all three anions can act as CA substrates. In this paper we prove experimentally that none of them may act as substrates of CA and propose an explanation to the above controversy, discussing the mode of binding of small molecules within the enzyme active site.

Ammonia↗
PubMed1993

Binding of cyanide, cyanate, and thiocyanate to human carbonic anhydrase II.

Computer simulation techniques are used to address the question of how cyanide and related ions interact with human carbonic anhydrase II (HCAII). Spectroscopic results have suggested that cyanide is coordinated with the zinc ion, while recent X-ray results suggest that the cyanide ion is noncovalently associated with the zinc-water or zinc-hydroxide form of the enzyme. We have carried out simulations on three models in an attempt to shed light on why the spectroscopic and X-ray results differ. The first model we studied (Model I) has cyanide directly coordinated to the zinc ion, the second has it noncovalently interacting with the zinc-hydroxide (high pH) form of the enzyme (Model II), and the third has cyanide noncovalently interacting with the zinc-water (low pH) form of the enzyme (Model III). None of these models is satisfactory in explaining the available structural data obtained from X-ray crystallography. This leads us to propose an alternative model, in which HCAII hydrates HCN to form an OH-/HCN complex coordinated to the Zn ion. Ab initio calculations are consistent with this model. Based on these results we are able to explain the observed crystallographic behavior of cyanate and, by inference, thiocyanate.

Bicarbonates↗
PubMed1984

Effect of administration of sodium cyanate and melphalan on the lifespan of P388 tumor-bearing CD2F1 mice.

Sodium cyanate (NaOCN) at a dose of 250 mg/kg was shown to decrease protein synthesis in P388 leukemia tumor cells to approximately 52% of control values at 2 h and 32% at 5 h after NaOCN administration, without a corresponding decrease in various normal tissues of the tumor-bearing CD2Fl mice. CD2Fl mice that had received P388 tumor cells IP 1 day prior to drug administration underwent various schedules of treatment with NaOCN and melphalan (MLN). NaOCN (200 mg/kg or 250 mg/kg) administered IP has no significant antitumor activity (increased mean lifespan [ILS] less than 20%). The simultaneous IP administration of NaOCN (250 mg/kg) plus MLN (15 mg/kg) resulted in a significantly greater antitumor activity (approximately 265% of control, with 21 of 30 animals being long-term survivors) than MLN (15 mg/kg) alone (approximately 156% of control, with 11 of 30 animals being long-term survivors). This synergism was not observed when MLN was administered 4 h after NaOCN administration. The synergistic activity of MLN with NaOCN does not appear to be secondary to alterations in the absorption from the peritoneal cavity into the systemic circulation as determined by 3H2O. NaOCN does not increase the intracellular concentration of [chloroethyl-14C]MLN into P388 cells. The mechanism of the synergistic antitumor activity of simultaneous IP administration of NaOCN and MLN is unknown.

Absorption↗