Kinetics and thermodynamics of the formation of glucose arsenate. Reaction of glucose arsenate with phosphoglucomutase.
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Arsenic↗
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A long-term health examination upon lead arsenate workers in an insecticides factory. (Studies on lead arsenate poisoning, Part 2).
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Arsenic↗
Effect of arsenate on inorganic phosphate transport in Escherichia coli.
The effect of arsenate on strains dependent on the two major inorganic phosphate (Pi) transport systems in Escherichia coli was examined in cells grown in 1 mM phosphate medium. The development of arsenate-resistant Pi uptake in a strain dependent upon the Pst (phosphate specific transport) system was examined. The growth rate of Pst-dependent cells in arsenate-containing medium was a function of the arsenate-to-Pi ratio. Growth in arsenate-containing medium was not due to detoxification of the arsenate. Kinetic studies revealed that cells grown with a 10-fold excess of arsenate to Pi have almost a twofold increase in capacity (Vmax) for Pi, but maintained the same affinity (Km). Pi accumulation in the Pst-dependent strain was still sensitive to changes in the arsenate-to-Pi ratio, and a Ki (arsenate) for Pi transport of 39 microM arsenate was determined. The Pst-dependent strain did not accumulate radioactive arsenate, and showed only a transient decrease in intracellular adenosine triphosphate levels after arsenate was added to the medium. The Pi transport-dependent strain ceased growth in arsenate-containing media. This strain accumulated 74As-arsenate, and intracellular adenosine triphosphate pools were almost completely depleted after the addition of arsenate to the medium. Arsenate accumulation required a metabolizable energy source and was inhibited by N-ethylmaleimide. Previously accumulated arsenate could exchange with arsenate or Pi in the medium.
Adenosine Triphosphate↗
Coprecipitation of arsenate with metal oxides: nature, mineralogy, and reactivity of aluminum precipitates.
Arsenic mobilization in soils is mainly controlled by sorption/desorption processes, but arsenic also may be coprecipitated with aluminum and/or iron in natural environments. Although coprecipitation of arsenic with aluminum and iron oxides is an effective treatment process for arsenic removal from drinking water, the nature and reactivity of aluminum- or iron-arsenic coprecipitates has received little attention. We studied the mineralogy, chemical composition, and surface properties of aluminum-arsenate coprecipitates, as well as the sorption of phosphate on and the loss of arsenate from these precipitates. Aluminum-arsenate coprecipitates were synthesized at pH 4.0, 7.0, or 10.0 and As/Al molar ratio (R) of 0, 0.01, or 0.1 and were aged 30 or 210 d at 50 degrees C. In the absence of arsenate, gibbsite (pH 4.0 or 7.0) and bayerite (pH 10.0) formed, whereas in the presence of arsenate, very poorly crystalline precipitates formed. Short-range ordered materials (mainly poorly crystalline boehmite) formed at pH 4.0 (R = 0.01 and 0.1), 7.0, and 10.0 (R= 0.1) and did not transform into Al(OH)3 polymorphs even after prolonged aging. The surface properties and chemical composition of the aluminum precipitates were affected by the initial pH, R, and aging. Chemical dissolution of the samples by 6 mol L(-1) HCl and 0.2 mol L(-1) oxalic acid/ oxalate solution indicated that arsenate was present mainly in the short-range ordered precipitates. The sorption of phosphate onto the precipitates was influenced by the nature of the samples and the amounts of arsenate present in the precipitates. Large amounts of phosphate partially replaced arsenate only from the samples formed at R = 0.1. The quantities of arsenate desorbed from these coprecipitates by phosphate increased with increasing phosphate concentration, reaction time, and precipitate age butwere always lessthan 30% of the amounts of arsenate present in the materials and were particularly low (<4%) from the sample prepared at pH 4.0. Arsenate appeared to be occluded within the network of short-range ordered materials and/or sorbed onto the external surfaces of the precipitates, but sorption on the external surfaces seemed to increase by increasing pH of sample preparation and aging. Furthermore, at pH 4.0 more than in neutral or alkaline systems the formation of aluminum arsenate precipitates seemed to be favored. Finally, we have observed that greater amounts of phosphate were sorbed on an aluminum-arsenate coprecipitate than on a preformed aluminum oxide equilibrated with arsenate under the same conditions (R = 0.1, pH 7.0). In contrast, the opposite occurred for arsenate desorption, which was attributed to the larger amounts of arsenate occluded in the coprecipitate.
Adsorption↗
High intracellular phosphorus contents exhibit a correlation with arsenate resistance in chlamydomonas mutants.
Pi in the medium relieved the toxicity of arsenate against cellular growth of Chlamydomonas reinhardtii. To investigate the relationship between intracellular P contents and arsenate resistance, we determined the intracellular P contents of arsenate-sensitive and arsenate-resistant mutants, which had been generated by random insertional mutagenesis. All 13 arsenate-resistant mutants showed higher P contents than the parent strain, while arsenate-sensitive mutants with high P contents were not found. In one of the arsenate-resistant mutants, AR3, the intracellular P content was about twice that in the wild type during growth in the absence of arsenate. Arsenate incorporation in AR3 was suppressed within 10 min after the addition of 1 mM arsenate, while Pi incorporation continued even after arsenate uptake ceased. Whereas the P content of the wild type decreased to half in the presence of 0.5 mM arsenate, almost the same degree (about 50%) of decrease was observed in AR3 cells grown in the presence of as much as 3 mM arsenate. AR3, in which PTB1, a homolog of a Pi transporter gene, had been disrupted, exhibited a higher activity of a high-affinity Pi transporter, suggesting that it may be due to a compensatory transport activity. These data suggest that the intracellular level of P is one of the important factors of arsenate resistance.
Animals↗
Inducible plasmid-determined resistance to arsenate, arsenite, and antimony (III) in escherichia coli and Staphylococcus aureus.
Plasmids in both Escherichia coli and Staphylococcus aureus contain an "operon" that confers resistance to arsenate, arsenite, and antimony(III) salts. The systems were always inducible. All three salts, arsenate, arsenite, and antimony(III), were inducers. Mutants and a cloned deoxyribonucleic acid fragment from plasmid pI258 in S. aureus have lost arsenate resistance but retained resistances to arsenite and antimony, demonstrating that separate genes are involved. Arsenate-resistant arsenite-sensitive S. aureus plasmid mutants were also isolated. In E. coli, plasmid-determined arsenate resistance and reduced uptake were additive to that found with chromosomal arsenate resistance mutants. Arsenate resistance was due to reduced uptake of arsenate by the induced plasmid-containing cells. Under conditions of high arsenate, when some uptake could be demonstrated with the induced resistant cells, the arsenate was rapidly lost by the cells in the absence of extracellular phosphate. Sensitive cells retained arsenate under these conditions. When phosphate was added, phosphate-arsenate exchange occurred. High phosphate in the growth medium protected cells from arsenate, but not from arsenite or antimony(III) toxicity. We do not know the mechanisms of arsenite or antimony resistance. However, arsenite was not oxidized to less toxic arsenate. Since cell-free medium "conditioned" by prior growth to induced resistant cells with toxic levels of arsenite or antimony(III) retained the ability to inhibit the growth of sensitive cells, the mechanism of arsenite and antimony resistance does not involve conversion of AsO2- or SbO+ to less toxic forms or binding by soluble thiols excreted by resistant cells.
Antimony↗
Dissimilatory arsenate reduction by a facultative anaerobe, Bacillus sp. strain SF-1.
Bacillus sp. strain SF-1, isolated first as a selenate-reducing bacterium, was characterized as a novel arsenate-reducing bacterium. Strain SF-1 rapidly reduced 10 mM levels of arsenate to arsenite with concomitant cell growth and lactate oxidation under anoxic conditions, indicating that arsenate can act as the terminal electron acceptor for anaerobic respiration (dissimilatory arsenate reduction). Strain SF-1 can use various organic compounds including synthetic sewage mainly composed of peptone and meat extract as the electron donors for arsenate reduction. Although strain SF-1 can grow aerobically, which is very rare for dissimilatory arsenate-reducing bacteria, the presence of oxygen inhibited the arsenate reduction. On the other hand, the presence of nitrate or selenate, which can support the growth of strain SF-1 as electron acceptors, did not significantly inhibit the arsenate reduction. Arsenate-reducing activity, that is, arsenate reductase, was exhibited in strain SF-1 only when grown on arsenate, but the enzyme could not reduce other oxyanions including nitrate and selenate. It was presumed that arsenate reduction was carried out by an enzyme system separate from those of nitrate and selenate reduction, and the arsenate reductase was inducible and specific for arsenate. These results suggest that strain SF-1 may be utilized for extracting arsenic from contaminated soil for the purpose of bioremediation.
Journal Article↗
Electrochemical and spectroscopic study of arsenate removal from water using zero-valent iron media.
This study investigated the mechanisms involved in removing arsenate from drinking water supplies using zero-valent iron media. Batch experiments utilizing iron wires suspended in anaerobic arsenate solutions were performed to determine arsenate removal rates as a function of the arsenate solution concentration. Corrosion rates of the iron wires were determined as a function of elapsed time using Tafel analysis. The removal kinetics in the batch reactors were best described by a dual-rate model in which arsenate removal was pseudo-first-order at low concentrations and approached zero-order in the limit of high arsenate concentrations. The presence of arsenate decreased iron corrosion rates as compared to those in blank 3 mM CaSO4 background electrolyte solutions. However, constant corrosion rates were attained after approximately 10 days elapsed, indicating that the passivation processes had reached steady state. The cathodic Tafel slopes were the same in the arsenate and the blank electrolyte solutions. This indicates that water was the primary oxidant for iron corrosion and that arsenate did not directly oxidize the iron wires. The anodic Tafel slopes were greater in the arsenate solutions, indicating that arsenate formed complexes with iron corrosion products released at anodic sites on the iron surfaces. Ion chromatography analyses indicated that there was no measurable reduction of As(V) to As(III). X-ray absorption spectroscopy analyses indicated that all arsenic associated with the zero-valent iron surfaces was in the oxidation state. Interatomic arsenic-iron distances determined from EXAFS analyses were consistent with bidentate corner-sharing among arsenate tetrahedra and iron octahedra. Results from this study show that under conditions applicable to drinking water treatment, arsenate removal by zero-valent iron media involves surface complexation only and does not involve reduction to metallic arsenic.
Arsenates↗
A novel arsenate reductase from the arsenic hyperaccumulating fern Pteris vittata.
Pteris vittata sporophytes hyperaccumulate arsenic to 1% to 2% of their dry weight. Like the sporophyte, the gametophyte was found to reduce arsenate [As(V)] to arsenite [As(III)] and store arsenic as free As(III). Here, we report the isolation of an arsenate reductase gene (PvACR2) from gametophytes that can suppress the arsenate sensitivity and arsenic hyperaccumulation phenotypes of yeast (Saccharomyces cerevisiae) lacking the arsenate reductase gene ScACR2. Recombinant PvACR2 protein has in vitro arsenate reductase activity similar to ScACR2. While PvACR2 and ScACR2 have sequence similarities to the CDC25 protein tyrosine phosphatases, they lack phosphatase activity. In contrast, Arath;CDC25, an Arabidopsis (Arabidopsis thaliana) homolog of PvACR2 was found to have both arsenate reductase and phosphatase activities. To our knowledge, PvACR2 is the first reported plant arsenate reductase that lacks phosphatase activity. CDC25 protein tyrosine phosphatases and arsenate reductases have a conserved HCX5R motif that defines the active site. PvACR2 is unique in that the arginine of this motif, previously shown to be essential for phosphatase and reductase activity, is replaced with a serine. Steady-state levels of PvACR2 expression in gametophytes were found to be similar in the absence and presence of arsenate, while total arsenate reductase activity in P. vittata gametophytes was found to be constitutive and unaffected by arsenate, consistent with other known metal hyperaccumulation mechanisms in plants. The unusual active site of PvACR2 and the arsenate reductase activities of cell-free extracts correlate with the ability of P. vittata to hyperaccumulate arsenite, suggesting that PvACR2 may play an important role in this process.
Amino Acid Motifs↗
Induction of proliferative lesions of the uterus, testes, and liver in swiss mice given repeated injections of sodium arsenate: possible estrogenic mode of action.
Inorganic arsenic (As) is a human carcinogen but has not been unequivocally proven carcinogenic in rodents. For instance, one older study indicates that repeated iv injections of sodium arsenate might induce lymphomas in Swiss mice (58% incidence) (Osswald and Goerttler, Verh. Dtsch. Ges. Pathol. 55, 289-293, 1971), but it was considered inadequate for critical evaluation of carcinogenic potential largely because of issues in experimental design. Therefore, we studied repeated iv sodium arsenate injection and neoplastic response in male and female Swiss mice. Groups (n = 25) of mice received sodium arsenate (0.5 mg/kg, iv) or saline (control) once/week for 20 weeks and were observed for a total of 96 weeks when the study ended. Differences in survival and body weights were unremarkable. In females, arsenate induced marked increases in the incidence and severity of cystic hyperplasia of the uterus compared against controls. Arsenate also was associated with a rare adenocarcinoma of the uterus. Hyperplastic uterine epithelium from arsenate-exposed animals showed strong positive immunostaining for the proliferating cell nuclear antigen (PCNA). There was also an upregulation of estrogen receptor (ER) immunoreactive protein in the early lesions of uterine luminal and glandular hyperplasia, although a progressive decrease in its expression was seen in the severe hyperplastic or neoplastic epithelium. In common with the preneoplastic and neoplastic gynecological lesions in humans, the levels of immunoreactive inducible nitric oxide synthase (iNOS) and 3-nitrotyrosine-containing proteins were greater in the uterine hyperplastic epidermis and their intensity was positively correlated with the severity of the lesions. Arsenate-induced uterine hyperplastic lesions also showed a strong upregulation of cyclin D1, an estrogen-associated gene product essential for progression through the G1 phase of the cell cycle. In other tissues, arsenate increased testicular interstitial cell hyperplasia incidence and severity over control but without affecting the incidence of tubular degeneration. Arsenate also induced increases in hepatic proliferative lesions (HPL; foci of alteration + neoplasia), but only in females. Significant skin changes (incidence of hyperkeratotic lesions) and renal lesions (severity of nephropathy) also occurred in arsenate-treated females. Thus, repeated arsenate exposure, though not outright tumorigenic in the present study, was associated with proliferative, preneoplastic lesions of the uterus, testes, and liver. Estrogen treatment has been associated with proliferative lesions and tumors of the uterus, female liver, and testes in other studies, supporting a hypothesis that arsenate might somehow act through an estrogenic mode of action.
Animals↗
Arsenate substitutes for phosphate in the human red cell sodium pump and anion exchanger.
The sodium pump of human red blood cells mediates a Rb:Rb exchange that is dependent for maximal rates upon the simultaneous presence of intracellular ATP (or ADP) and phosphate. We have measured ouabain-sensitive 86Rb uptake into resealed ghosts of human red cells containing ADP and show that arsenate will substitute for phosphate in supporting the Rb:Rb exchange transport mode. The concentration dependence of arsenate-supported Rb:Rb exchange in ghosts containing 2 mM ADP shows both activating and inhibiting phases; the dependence upon phosphate shows similar characteristics. Elevation of the external [Rb] lowers the apparent affinity for arsenate since there is a shift to higher concentrations of arsenate in the activating and inhibiting phases of the arsenate concentration dependence curve. Similarly, elevation of [ADP] substantially reduces the inhibition of Rb:Rb exchange observed at higher [arsenate]. These effects are also observed in phosphate-supported Rb:Rb exchange. The phosphate requirement for Rb:Rb exchange involves phosphorylation of the sodium pump protein; the close agreement between the effects of arsenate and phosphate in supporting Rb:Rb exchange makes it likely that arsenylation of the sodium pump occurs during Rb:Rb exchange. Arsenate efflux from red blood cell ghosts into arsenate-free chloride medium is partially inhibited (77-80%) by DNDS (4,4'-dinitro-2,2'-stilbenedisulfonic acid), this compares with 82-87% inhibition by DNDS of phosphate efflux under the same conditions. It appears that Band III, the red cell anion transport system, accepts arsenate in a similar fashion to phosphate and that a fraction of the flux of both anions may occur through pathways other than Band III. Thus, in human red blood cells, both the sodium pump and the anion exchange transport system will accept arsenate as a phosphate congener and the protein-arsenate interactions are very similar to those with phosphate.
Arsenates↗
Synthesis and hydrolysis of ADP-arsenate by beef heart submitochondrial particles.
The kinetic parameters for inorganic phosphate and inorganic arsenate as substrates for the synthesis of ATP and ADP-arsenate, respectively, by beef heart submitochondrial particles have been determined. The Vm and Km values for arsenate and phosphate, as well as the Km values for ADP in the two reactions, are the same within experimental error of the measurements. These data are consistent with covalent bond formation not being the rate-limiting step for either ATP or ADP-arsenate synthesis. The hydrolysis of ATP and of ADP-arsenate was studied under conditions of net synthesis of ATP or ADP-arsenate. The apparent first order rate constant for ATP hydrolysis increased with submitochondrial particle concentration, indicating that hydrolysis of ATP was catalyzed by the submitochondrial particle preparation. Nonenzymic hydrolysis of ATP was negligible compared to enzymic hydrolysis. The apparent first order rate constant for ADP-arsenate hydrolysis did not vary with submitochondrial particle concentration, indicating that ADP-arsenate hydrolysis was nonenzymic. Enzymic hydrolysis of ADP-arsenate was too slow, compared with its rapid nonenzymic hydrolysis, to be detected. The first order rate constant for ADP-arsenate hydrolysis at pH 7.5, 30 degrees C, was determined to be greater than 5 min-1 and was estimated to be 70 min-1. These data confirm previous suggestions that arsenate "uncouples" oxidative phosphorylation by a mechanism involving synthesis of ADP-arsenate, followed by its rapid nonenzymic hydrolysis.
Adenosine Diphosphate↗
Facile reduction of arsenate in methanogenic sludge.
Due to the recent enactment of a stricter drinking water standard for arsenate, large quantities of arsenate-laden drinking water residuals will be disposed in municipal landfills. The objective of this study was to determine the role of methanogenic consortia on the conversion of arsenate. Methanogenic conditions commonly occur in mature municipal solid waste landfills. The results indicate the rapid and facile reduction of arsenate to arsenite in methanogenic sludge. Endogenous substrates in the sludge were sufficient to support the reductive biotransformation. However the rates of arsenate reduction were stimulated by the addition of exogenous electron donating substrates, such as H2, lactate or a mixture of volatile fatty acids. A selective methanogenic inhibitor stimulated arsenate reduction in microcosms supplied with H2, suggesting that methanogens competed with arsenate reducers for the electron donor. Rates of arsenate reduction increased with arsenate concentration up to 2 mM, higher concentrations were inhibitory. The electron shuttle, anthraquinone-2,6-disulfonate, used as a model of humic quinone moieties, was shown to significantly increase rates of arsenate reduction at substoichiometric concentrations. The presence of sulfur compounds, sulfate and sulfide, did not affect the rate of arsenate transformation but lowered the yield of soluble arsenite, due to the precipitation of arsenite with sulfides. The results taken as a whole suggest that arsenate disposed into anaerobic environments may readily be converted to arsenite increasing the mobility of arsenic. The extent of the increased mobility will depend on the concentration of sulfides generated from sulfate reduction.
Anthraquinones↗
Relationship between phospholipid biosynthesis and the efficiency of the arsenate transport system in yeasts.
In studying the possibility that phosphoinositides which formed complexes with arsenic were involved in the arsenate transport system of yeasts, a comparative study of the phospholipid composition and metabolism was carried out both in Saccharomyces carslbergensis and in its arsenate-adapted variant, which showed a deficient inflow of arsenate. It was found that the lipid composition of the two organisms was quite similar, the main classes of phospholipids being phosphatidylcholine, phosphatidylethanolamine, and phosphoinositides. The only difference was a 1.5- to 2-fold increase in the proportion of inositides in the arsenate-adapted cells. When the transport of arsenate became inactivated in the nonadapted yeasts after a 30- to 60-min exposure to 10(-2)m arsenate, an increment of inositides of 29 to 50% over the original level was also detected. A study of the incorporation of radioactivity from uniformly labeled (14)C-maltose and from (32)P-orthophosphate ((32)P(i)) demonstrated a decreased rate of lipid biosynthesis in the arsenate-adapted cells as compared to the normal nonadapted ones. The turnover of the phosphate in phospholipids demonstrated no turnover in phosphatidylcholine and phosphatidylethanolamine, and a slow turnover in phosphoinositides. It could be inferred that a normal rate of phospholipid (phosphoinositides) biosynthesis is necessary to have a normal arsenate uptake and that inositide accumulation impairs both the mechanism responsible for the uptake and accumulation of arsenate and the rate of lipid biosynthesis. No differences were found in the deoxyribonucleic acid or protein content of the two types of cells. Also, the arsenate-adapted cells, once freed of external arsenate, showed an increased uptake of (32)P(i) from low external concentrations of phosphate (10(-6) to 10(-8)m, 10-fold over that observed in AsS cells). These results are indicative of independent behavior in phosphate and arsenate transport systems.
Arsenic↗
Interaction of arsenate with phosphate-transport systems in wild- type and mutant Streptococcus faecalis.
Harold, F. M. (National Jewish Hospital, Denver, Colo.), and J. R. Baarda. Interaction of arsenate with phosphate-transport systems in wild-type and mutant Streptococcus faecalis. J. Bacteriol. 91:2257-2262. 1966.-Arsenate competitively inhibits the growth of Streptococcus faecalis, primarily by competition with phosphate for a common transport system. Arsenate is itself accumulated by the cells; the uptake requires metabolic energy, and the intracellular arsenate level may reach 0.01 m. Cells loaded with arsenate have lost the capacity to take up radioactive glutamate, rubidium, phosphate, or arsenate itself, apparently by the uncoupling of adenosine triphosphate generation. The pH dependence of arsenate uptake is complex. At low concentrations of extracellular arsenate, uptake by the wild-type strain 9790 exhibits a single maximum about pH 8; mutant PT-1, previously shown to be defective in phosphate uptake, takes up essentially no arsenate. At high concentrations of arsenate, uptake by the wild type is bimodal with maxima at pH 5.5 and 9; the uptake curve for mutant PT-1 corresponds to the shoulder in the curve for the wild type. The apparent dissociation constant for arsenate uptake by the wild type is approximately 10(-5)m from pH 5 to 9, whereas that for mutant PT-1 is about 5 x 10(-5) M at pH 5 and rises rapidly with increasing pH. The results confirm the earlier conclusion that the lesion in mutant PT-1 resides in the transport of phosphate and arsenate. It is proposed that the wild type has two distinct transport systems, whereas the mutant has lost the one with alkaline pH optimum.
Adenosine Triphosphate↗
Subchronic dispositional and toxicological effects of arsenate administered in drinking water to mice.
Exposure to the drinking water contaminant arsenate is a daily occurrence and there are concerns that this exposure may lead to cancer. Although the acute dispositional effects of arsenate have been studied in detail, there is minimal information on the disposition and toxicological effects of it after continuous exposure. The objective of this study was to examine in mice the effect of a 4-wk treatment with arsenate administered in drinking water. Female B6C3F1 mice (3/cage) were housed in metabolism cages and given water and food ad libitum. Two groups (A, B) of mice were treated (4 cages/treatment/group) with distilled water (control, C) or water containing 0.025 mg/L (L) or 2.5 mg/L (H) arsenate. Group A was sacrificed on d 28 and plasma and urine samples were taken for determination of clinical chemistry parameters. Liver and kidney tissue samples were taken for histopathological analysis. The reduced nonprotein sulfhydryl (NPSH) content in several tissues was determined. Group B was gavaged with [73As]arsenate on d 28 and continued the arsenate drinking water exposure for 48 h. Excreta and tissues were collected and analyzed for 73As. Urine was further analyzed for arsenate and its metabolites. There were no effects on the mean daily amount of water and food consumed, whereas the mean daily urine volume excreted was significantly elevated by 10% in the H-treated animals compared to C and L. A dose-related hepatic vacuolar degeneration in the liver was observed, but no histological changes were evident in the kidney. Only clinical chemistry parameters in plasma were altered by the arsenate treatment. Glucose was significantly lower at the H dose compared to C and L, triglycerides were significantly greater in C than L and H, and creatinine was significantly greater in H than C. Hepatic NPSH content in the H animals was significantly lower than C and L animals, whereas no effects in lung and kidney were detected. The weights of liver, lung, and kidney, as well as their tissue/body weight ratios, were significantly decreased in the H animals. 73As was primarily eliminated in urine, and its elimination was not affected by dose. No effects on the 48-h 73As cumulative excretion (urine+fecal) were detected. The 73As distribution was low in amount and widely dispersed throughout the animal (< 3% of the 73As dose). The kidney had the highest 73As concentration of the tissues (0.01% 73As dose/g tissue). Dimethylarsinic acid was the major metabolite detected in urine, with lower amounts of arsenate arsenite, and monomethylarsonate. There were no differences between the treatment groups in the amount of urinary metabolites after a single dose of [73As]arsenate. Several toxicological effects were observed in animals administered arsenate in drinking water, but no changes in the disposition of this arsenical were detected at the doses used in this study.
Administration, Oral↗
Phosphate (Pi) and arsenate uptake by two wheat (Triticum aestivum) cultivars and their doubled haploid lines.
BACKGROUND AND AIMS: Arsenic accumulation in cereal crops represents an important pathway for human exposure to arsenic from the environment. The objectives of the present work were to find whether the relationship between arsenate and phosphate (Pi) uptake rate differs among genotypes and to select genotypes with a low arsenate uptake rate with the aim of improving food safety and human health. METHODS: A hydroponic experiment was conducted using two wheat (Triticum aestivum) cultivars (Hanxuan 10 and Lumai 14) and ten doubled haploid (DH) lines derived from them to investigate Pi and arsenate uptake over 48 h. Ten plants were transferred to bottles containing 50 mL of pre-treatment solution containing 0.5 mM CaCl2 and 5 mM MES set at pH 6.0 with 330 microM Pi as KH2PO4 and 7.33 microM arsenate. The solutions were aerated continuously. At 8, 24 and 48 h after uptake, 1 mL of test solution was sampled for determination of Pi and arsenate concentrations. KEY RESULTS AND CONCLUSIONS: For each wheat line, Pi and arsenate concentrations in the test solution decreased with uptake time. Exponential (for Pi) or polynomial (for arsenate) regression plots fitted the data closely. For all genotypes, net Pi uptake rates decreased with time (from 0 to 48 h). However, net arsenate uptake rates decreased with time for D5, changed little with time for the male parent, D4 and D6, and increased with time for the others. An inflexion of about 25 microm Pi was observed for the relationship between arsenate and Pi concentrations in the test solution, indicating that 25 microm could be the point where the high-affinity uptake system 'switches on', or dominates over low-affinity uptake. In addition, the male parent, D1, D6 and D10 were considered ideal genotypes because they possess Pi transporters that discriminate strongly against arsenate and are expected to accumulate less arsenate in the field.
Arsenates↗
Purification and characterization of the respiratory arsenate reductase of Chrysiogenes arsenatis.
Chrysiogenes arsenatis is the only bacterium known that respires anaerobically using arsenate as the terminal electron acceptor and the respiratory substrate acetate as the electron donor. During growth, the arsenate is reduced to arsenite; the reduction is catalyzed by an arsenate reductase. This study describes the purification and characterization of a respiratory arsenate reductase (Arr). The enzyme consists of two subunits with molecular masses of 87 kDa (ArrA) and 29 kDa (ArrB), and is a heterodimer alpha1beta1 with a native molecular mass of 123 kDa. The arsenate reductase contains molybdenum, iron, acid-labile sulfur and zinc as cofactor constituents. The Km of the enzyme for arsenate is 0.3 mM and the Vmax is 7013 micromol arsenate reduced x min(-1) x mg protein(-1). Nitrate, sulfate, selenate and fumarate cannot serve as alternative electron acceptors for the arsenate reductase. Synthesis of the protein is regulated, as arsenate must be present during growth for the enzyme to be fully induced. The N-terminus of ArrA is similar to a number of procaryotic molybdenum-containing polypeptides (e.g. the formate dehydrogenases H and N of Escherichia coli). The N-terminus of ArrB is similar to iron-sulfur proteins. The respiratory arsenate reductase of C. arsenatis is different from the non-respiratory arsenate reductases of E. coli and Staphylococcus aureus.
Adenosine Triphosphatases↗