Disease relevance of dioxidoarsinic acid

• Plasmid-determined arsenate resistance from plasmid pl258 encoded by genes arsR, arsB, and arsC was evolved in Escherichia coli [1].
• Most strains were phage group I or nontypable strains related to them and were resistant only to penicillin, cadmium, and arsenate [2].
• We report here that decreased net uptake results from accelerated efflux of arsenate by induced plasmid-containing cells of Staphylococcus aureus and Escherichia coli [3].
• Bacillus subtilis arsenate reductase is structurally and functionally similar to low molecular weight protein tyrosine phosphatases [4].
• Here we show that a two-gene cluster (arrAB; arsenate respiratory reduction) in the bacterium Shewanella sp. strain ANA-3 specifically confers respiratory As(V) reductase activity [5].

Psychiatry related information on dioxidoarsinic acid

• Adsorption of arsenate by all soils was strongly kinetic, where the rate of As(V) retention was rapid initially and was followed by gradual or somewhat slow retention behavior with increasing reaction time [6].
• This depression appears to be more pronounced, under strictly comparable conditions, when arsenate is used to stimulate ATP synthase activity than when the ornithine-citrulline conversion reaction is used for the same purpose [7].

High impact information on dioxidoarsinic acid

• This is exemplified by the uptake of phosphate or its close analogue arsenate by bacterial cells by way of a high affinity active transport system dependent on a phosphate-binding protein; this system is unable to recognize other inorganic oxyanions and is, moreover, distinct from the one for sulphate transport [8].
• In suspensions of tubules, arsenate increased oxygen consumption rates by 20.5 +/- 2.9% and decreased NADH fluorescence by 10.8 +/- 1.5% [9].
• Arsenate induces stress proteins in cultured rat myoblasts [10].
• Mutation of the Arabidopsis thaliana PHOSPHATE TRANSPORTER TRAFFIC FACILITATOR1 (PHF1) impairs Pi transport, resulting in the constitutive expression of many Pi starvation-induced genes, increased arsenate resistance, and reduced Pi accumulation [11].
• Arabidopsis thaliana plants transformed with the arsC gene expressed from a light-induced soybean rubisco promoter (SRS1p) strongly express ArsC protein in leaves, but not roots, and were consequently hypersensitive to arsenate [12].

Chemical compound and disease context of dioxidoarsinic acid

• Reduction of arsenate to arsenite by the ArsC protein of the arsenic resistance operon of Staphylococcus aureus plasmid pI258 [13].
• The crystal structure of Bacillus subtilis arsenate reductase in the reduced form with a bound sulfate ion in its active site is solved at 1.6-A resolution [4].
• It was found that in addition to being ampicillin sensitive this mutant was hypersensitive to arsenate, which may be connected with the fact that the gor gene maps between 77 and 78 min on the E. coli genome, close to the pit locus encoding the major arsenate transport system of E. coli [14].
• Depletion of cellular glutathione (GSH) with L-buthionine-SR-sulfoximine (BSO), increased the incidence of chromosomal aberrations induced by arsenite, arsenate and MAA, and markedly suppressed the clastogenic effects of DMAA [15].
• Sodium arsenate was less effective than sodium perchlorate in causing thyroid histopathologies, but transient responses were seen for hypertrophy, hyperplasia, and colloid depletion (% colloid) [16].

Biological context of dioxidoarsinic acid

• Molecular evolution of an arsenate detoxification pathway by DNA shuffling [1].
• Expression of ACR2 cDNA in Escherichia coli complemented the arsenate-resistant and arsenate-sensitive phenotypes of various bacterial ars operon mutants [17].
• Conversion of I to III occurs by activation of phosphorylase either by formation of a ternary complex of phosphorylase b with effector and arsenate or, more efficiently, by direct phosphorylation to give the a form of the enzyme [18].
• Plasmid R773, which codes for resistances to arsenate, arsenite, and antimony, was introduced into Escherichia coli strain AN120, a mutant deficient in the H+-translocating ATPase of oxidative phosphorylation [19].
• These results provide evidence that ArsC from pI258 evolved from LMW PTPase by the grafting of a redox function onto a pre-existing catalytic site and that its evolutionary origin is different from those of arsenate reductases from Escherichia coli plasmid R773 and from Saccharomyces cerevisiae [20].

Anatomical context of dioxidoarsinic acid

• 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 [21].
• Addition of high concentrations (>1 mm) of inorganic phosphate (Pi) or arsenate to Ca2+-loaded mitochondria was followed by increased rates of H2O2 production, membrane lipid peroxidation, and swelling [22].
• Here we report that the levels of Prx I mRNA and protein are dramatically increased in a murine osteoblast cell line, MC3T3-E1, by treatment with sodium arsenate [23].
• In both sarcoplasmic reticulum and platelet vesicles, the effect of arsenate was antagonized by thapsigargin (2 microM), micromolar Ca2+ concentrations, P(i) (5-20 mM), and MgATP (10-100 microM) [24].
• Unlike other known inhibitors of brush border membrane (BBM) transport of Pi, e.g. arsenate, NAD, and ethane-1-hydroxy-1,1-diphosphonate, PFA and PAA had no inhibitory effect on BBM-bound or solubilized alkaline phosphatase [25].

Associations of dioxidoarsinic acid with other chemical compounds

• Endogenous plant arsenate reductase (ACR) activity converts arsenate to arsenite in roots, immobilizing arsenic below ground [17].
• Vanadate and arsenate augmented the transfer reaction 200- and 2.5-fold, respectively, and lowered the pH optimum of the reaction [26].
• A "triple cysteine redox relay" is proposed for the arsenate reduction mechanism [4].
• The increase was measured in cells kept without glucose and with arsenate, where greater than 95% of intracellular radioactivity was recovered as free unesterified oleate [27].
• The mechanism proposed here for the catalysis of arsenate reduction by pI258 ArsC involves a nucleophilic attack by Cys 10 on arsenate, the formation of a covalent intermediate and the transport of oxidative equivalents by a disulfide cascade [20].

Gene context of dioxidoarsinic acid

• While arsC, the arsenate reductase gene, contained no mutations, its expression level was increased, and the rate of arsenate reduction was increased 12-fold [1].
• Disruption of the GTR1 gene resulted in slow growth at 30 degrees C and no growth at 15 degrees C; other phenotypes resembled those of pho84 mutants and included constitutive synthesis of repressible acid phosphatase, reduced Pi transport activity, and resistance to arsenate [28].
• In this study, we demonstrate that ACR2 complemented the arsenate-sensitive phenotype of an arsC deletion in Escherichia coli [29].
• Directed evolution of a yeast arsenate reductase into a protein-tyrosine phosphatase [30].
• The presence of ACR3 together with ACR2 on a multicopy plasmid was conducive to increased arsenate resistance [31].

Analytical, diagnostic and therapeutic context of dioxidoarsinic acid

• Laser Raman spectroscopy has been used to study a phosphate transfer reaction from ATP to Pi or arsenate in dimethyl sulfoxide [32].
• Titration of the intrinsic tryptophan fluorescence of the weakly active AroA mutant, Asp313Ala (D313A), demonstrated a fluorescence decrease upon enolpyruvyl shikimate 3-phosphate (EPSP) binding, and a further decrease upon binding of phosphate or arsenate to AroA_D313A.EPSP, suggesting a further conformational change [33].
• From other eyes retinas were isolated and maintained in organ culture, either untreated for 4 days maximum or for 21 hours during which the explants were treated the first 3 hours with selected doses of sodium arsenate or hydrogen peroxide [34].
• The level of resistance of the bacterial populations to arsenate was determined by the DVCMR bioassay, and the results showed a linear correlation with the total arsenic concentrations in the monitoring well water samples; no correlation was observed by culture methods with the methods employed [35].
• An arsenate reductase has been partially purified from human liver using ion exchange, molecular exclusion, hydroxyapatite chromatography, preparative isoelectric focusing, and electrophoresis [36].

References