Efficient enzymatic synthesis of phosphoroselenoate RNA by using adenosine 5'-(alpha-P-seleno)triphosphate.
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Acetaldehyde↗
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3'-(2,4-Dinitrobenzenesulfonyl)-2',7'-dimethylfluorescein as a fluorescent probe for selenols.
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Animals↗
[The synthesis of selenopyrylium salts (author's transl)].
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Chemical Phenomena↗
A non-radioactive and two radioactive assays for selenophosphate synthetase activity.
Selenophosphate synthetase catalyzes the formation of monoselenophosphate (SePO3(3-)) from ATP and selenide (reaction 1). [formula: see text] In one assay frequently used, [8-14C]AMP formation from [8-14C]ATP is estimated after separation of the nucleotides by thinlayer chromatography. An alternative non-radioactive assay in which the AMP product is estimated using AMP deaminase is described. The highly oxygen-labile selenophosphate product can be estimated in an assay employing [gamma-32P]ATP. The 32P-labeled selenophosphate is converted to [32P]orthophosphate by treatment with iodine and estimated after removal of residual [32P]ATP on charcoal.
Adenosine Monophosphate↗
Biosynthesis of selenophosphate.
Selenophosphate synthetase, the product of the selD gene, produces the highly active selenium donor, monoselenophosphate, from selenide and ATP. Positional isotope exchange experiments have shown hydrolysis of ATP occurs by way of a phosphoryl-enzyme intermediate. Although, mutagenesis studies have demonstrated Cys17 in the Escherichia coli enzyme is essential for catalytic activity the nucleophile in catalysis has not been identified. Recently, selenophosphate synthetase enzymes have been identified from other organisms. The human enzyme which contains a threonine residue corresponding to Cys17 in the E. coli enzyme, has been overexpressed in E. coli. The purified enzyme shows no detectable activity in the in vitro selenophosphate synthetase assay. In contrast, when the human enzyme is expressed to complement a selD mutation in E. coli, in the presence of 75Se, incorporation of 75Se into bacterial selenoproteins is observed. The inactive purified human enzyme together with the very low determined specific activity of the E. coli enzyme (83 nmol/min/mg) suggest an essential component for the formation of selenophosphate has not been identified.
Amino Acid Sequence↗
Utilization of selenocysteine as a source of selenium for selenophosphate biosynthesis.
Selenophosphate synthetase (SPS), the selD gene product from Escherichia coli, catalyzes the biosynthesis of monoselenophosphate from selenide and ATP. Characterization of selenophosphate synthetase revealed the determined K(m) value for selenide is far above the optimal concentration needed for growth and approached levels which are toxic. Selenocysteine lyase enzymes, which decompose selenocysteine to elemental selenium (Se(0)) and alanine, were considered as candidates for the control of free selenium levels in vivo. The ability of a lyase protein to generate Se(0) in the proximity of SPS maybe an attractive solution to selenium toxicity as well as the high K(m) value for selenide. Recently, three E. coli NifS-like proteins, CsdB, CSD, and IscS, were characterized. All three proteins exhibit lyase activity on L-cysteine and L-selenocysteine and produce sulfane sulfur, S(0), or Se(0) respectively. Each lyase can effectively mobilize Se(0) from L-selenocysteine for selenophosphate biosynthesis.
Adenosine Triphosphate↗
Plasma selenium in specific and non-specific forms.
Selenium is present in plasma and tissues in specific and non-specific forms. The experiments reported here were carried out to clarify some factors that affect these forms of the element in plasma. A selenium-replete human subject was given 400 microg of selenium daily for 28 days as selenomethionine and, in a separate experiment, as selenate. The selenomethionine raised plasma and albumin selenium concentrations. Selenate did neither. The molar ratio of methionine to selenium in albumin was approximately 8000 under basal and selenate-supplemented conditions but 2800 after selenomethionine supplementation. This demonstrates that selenium from selenomethionine, but not selenium from selenate, can be incorporated into albumin, presumably as selenomethionine in the methionine pool. Selenocysteine incorporation into albumin was studied in rats using (75)Se-selenocysteine. No evidence was obtained for incorporation of (75)Se into albumin after exogenous administration or endogenous synthesis of (75)Se-selenocysteine. Thus, selenocysteine does not appear to be incorporated non-specifically into proteins as is selenomethionine. These findings are in support of selenomethionine being a non-specific form of selenium that is metabolized as a constituent of the methionine pool and is unaffected by specific selenium metabolic processes. No evidence was found for non-specific incorporation of selenium into plasma proteins when it was administered as selenate or as selenocysteine. These forms of the element appear to be metabolized by specific selenium metabolic processes.
Adult↗
Selenium (Se) from high-selenium broccoli is utilized differently than selenite, selenate and selenomethionine, but is more effective in inhibiting colon carcinogenesis.
The reduction in incidence of chemically-induced colon cancer by foods high in selenium (Se) was investigated in Fisher-344 rats. The foods used were high-Se broccoli (produced in a greenhouse by addition of selenate to the media surrounding the plant roots) and a processed high-Se wheat product (made by milling high-Se wheat purchased from a seleniferous area). Weanling rats were fed diets containing different amounts of Se from these foods or from selenium salts (selenite and selenate). Early in the experiment the animals were injected with a chemical carcinogen. After 11 weeks on diets animals were killed and the colons examined for preneoplastic lesions (aberrant crypts foci, ACF). ACF were significantly reduced in animals fed supra-nutritional amounts of Se from broccoli, despite the finding that Se from broccoli was poorly bioavailable. Supra-nutritional amounts of Se from high-Se processed wheat also significantly reduced aberrant crypts (AC), although pure selenomethionine, (the predominant chemical form of Se in wheat), did not significantly reduce AC. These results emphasize the need to study Se in food forms, and not extrapolate from previous studies using pure chemical forms in cancer inhibition studies. They also demonstrate that foods with high Se bioavailability are not necessarily the most efficacious for cancer incidence reduction.
Animals↗
Removal of soluble selenium by a selenate-reducing bacterium Bacillus sp. SF-1.
In order to develop a biological process for removal of selenium from industrial wastewater, Bacillus sp. strain SF-1 was isolated from selenium-contaminated sediment. The bacterium reduces selenate to selenite and subsequently to nontoxic insoluble elemental selenium using lactate as an electron donor and selenate as an electron acceptor in an anaerobic condition. Elemental selenium transformed from soluble selenium was deposited both inside and outside of the cells. Since the selenate reduction rate of the strain SF-1 was higher than the selenite reduction rate, selenite was transiently accumulated. In an experiment of the repeated soluble selenium reduction by strain SF-1, 0.5 mM of selenate was sequentially treatable with a cycle of one day. Thus, our sequential system for removal of soluble selenium is very useful.
Bacillus↗
Laboratory-scale continuous reactor for soluble selenium removal using selenate-reducing bacterium, Bacillus sp. SF-1.
A model continuous flow bioreactor (volume 0.5 L) was constructed for removing toxic soluble selenium (selenate/selenite) of high concentrations using a selenate-reducing bacterium, Bacillus sp. SF-1, which transforms selenate into elemental selenium via selenite for anaerobic respiration. Model wastewater contained 41.8 mg-Se/L selenate and excess lactate as the carbon and energy source; the bioreactor was operated as an anoxic, completely mixed chemostat with cell retention time between 2.2-95.2 h. At short cell retention times selenate was removed by the bioreactor, but accumulation of selenite was observed. At long cell retention times soluble selenium, both selenate and selenite, was successfully reduced into nontoxic elemental selenium. A simple mathematical model is proposed to evaluate Se reduction ability of strain SF-1. First-order kinetic constants for selenate and selenite reduction were estimated to be 2.9 x 10(-11) L/cells/h and 5.5 x 10(-13) L/cells/h, respectively. The yield of the bacterial cells by selenate reduction was estimated to be 2.2 x 10(9) cells/mg-Se.
Bacillus↗
The functional role of selenocysteine (Sec) in the catalysis mechanism of large thioredoxin reductases: proposition of a swapping catalytic triad including a Sec-His-Glu state.
Thioredoxin reductases catalyse the reduction of thioredoxin disulfide and some other oxidised cell constituents. They are homodimeric proteins containing one FAD and accepting one NADPH per subunit as essential cofactors. Some of these reductases contain a selenocysteine at the C terminus. Based on the X-ray structure of rat thioredoxin reductase, homology models of human thioredoxin reductase were created and subsequently docked to thioredoxin to model the active complex. The formation of a new type of a catalytic triad between selenocysteine, histidine and a glutamate could be detected in the protein structure. By means of DFT (B3LYP, lacv3p**) calculations, we could show that the formation of such a triad is essential to support the proton transfer from selenol to a histidine to stabilise a selenolate anion, which is able to interact with the disulfide of thioredoxin and catalyses the reductive disulfide opening. Whereas a simple proton transfer from selenocysteine to histidine is thermodynamically disfavoured by some 18 kcal mol(-1), it becomes favoured when the carboxylic acid group of a glutamate stabilises the formed imidazole cation. An identical process with a cysteine instead of selenocysteine will require 4 kcal mol(-1) more energy, which corresponds to a calculated equilibrium shift of approximately 1000:1 or a 10(3) rate acceleration: a value close to the experimental one of about 10(2) times. These results give new insights into the catalytic mechanism of thioredoxin reductase and, for the first time, explain the advantage of the incorporation of a selenocysteine instead of a cysteine residue in a protein.
Animals↗
Combinatorial synthesis of an oligosaccharide library by using beta-bromoglycoside-mediated iterative glycosylation of selenoglycosides: rapid expansion of molecular diversity with simple building blocks.
A new method for constructing an oligosaccharide library composed of structurally defined oligosaccharides is presented based on an iterative glycosylation of selenoglycosides. Treatment of 2-acyl-protected selenoglycosides with bromine selectively generates beta-bromoglycosides, which serve as glycosyl cation equivalents in the oligosaccharide synthesis. Thus, the coupling of the bromoglycosides with another selenoglycoside affords the corresponding glycosylated selenoglycosides, which can be directly used to next glycosylation. The iteration of this sequence allows the synthesis of a variety of oligosaccharides including an elicitor active heptasaccharide. A characteristic feature of the iterative glycosylation is that glycosyl donors and acceptors with the same anomeric reactivity can be selectively coupled by activation of the glycosyl donor prior to coupling with the glycosyl acceptor. Therefore, same selenoglycosides can be used for both the glycosyl donors and the acceptors. This feature has been exemplified by a construction of an oligosaccharide library directed to elicitor-active oligosaccharides. The library composed of stereochemically defined oligoglucosides with considerable structural diversity can be constructed starting from simple selenoglycosides.
Carbohydrate Sequence↗
A computational study of thiolate and selenolate oxidation by hydrogen peroxide.
Ab initio molecular orbital calculations have been used to study the effects of the molecular environment on the oxidation of thiolate and selenolate by hydrogen peroxide. The reaction was first examined in vacuo at the QCISD(T)/6-311+G(2df,2pd)//MP2/6-311+G(d,p) level of theory. It was found for both thiolate and selenolate that a reactant aggregate is formed, which has a dissociation rate constant comparable to the activation rate constant (about 10(-3) s(-1) for thiolate and 10(-1) s(-1) for selenolate). Using the polarizable continuum model (PCM) it was then found that the dissociation barrier energy decreases dramatically in water giving a dissociation rate constant of the order of 10(9) s(-1). In this case, the predicted overall rate constant of the thiolate reaction was about 10.2 mol(-1) dm3 s(-1), which is in good agreement with the experimental rate constant of cysteine oxidation in aqueous solution. The calculated rate constant for the selenolate reaction was somewhat higher (about 35.4 mol(-1) dm3 s(-1)). However, this value is several orders of magnitude smaller than the experimental value reported for the oxidation of selenocysteine in glutathione peroxidase. By considering the effect of the PCM dielectric constant on the reaction rate constant it was concluded that the high reactivity of the selenocysteine in glutathione peroxidase, as compared with cysteine, could be mainly due to the molecular environment of the selenocysteine residue.
Hydrogen Peroxide↗
Capillary electrophoresis on-line coupled with hydride generation-atomic fluorescence spectrometry for speciation analysis of selenium.
A new method for speciation analysis of two inorganic selenium species was developed by on-line coupling of capillary electrophoresis (CE) with hydride generation-atomic fluorescence spectrometry (HG-AFS) and on-line conversion of Se(VI) to Se(IV). Baseline separation of Se(VI) and Se(IV) was achieved by CE in a 50 cm x 75 microm inside diameter (ID) fused-silica capillary at -20 kV using a mixture of 15 mmol.L(-1) NaH2PO4 and 0.5 mmol.L(-1) cetyltrimethylammonium bromide (pH 7.5) as electrolyte buffer. Se(VI) was on-line reduced to Se(IV) by mixing the CE effluent with concentrated HCl. The precision (relative standard deviation, RSD, n=7) ranged from 0.7 to 1.3% for migration time, 6.4 to 3.7% for peak height response, and 5.9 to 6.1% for peak area for the two selenium species at the 500 microg.L(-1) (as Se) level. The detection limits were 33 and 25 microg.L(-1) (as Se) for Se(VI) and Se(IV), respectively. The recoveries of the two selenium species in five locally collected water samples ranged from 88 to 114%. The developed method was applied to speciation analysis of inorganic selenium species in spiked natural water samples.
Electrophoresis, Capillary↗
Induction of cellular necrosis by the glutathione peroxidase mimetic ebselen.
The selenium-based compound ebselen is a powerful antioxidant, a potent anti-inflammatory agent and a potential neuroprotective compound. Several studies have demonstrated that part of the biological effect of ebselen is the result of the inhibition of apoptosis. We show in this report that ebselen induced the necrotic cell death of Sp2/0-Ag14 hybridoma cells. This process was rapid, with over 90% of the cells being dead after a 2 h exposure to 50 microM ebselen. The toxic effect of ebselen could not be prevented by the caspase inhibitor Z-VAD-fmk but could be blocked with thiol-containing compounds. Interestingly, ebselen addition completely prevented caspase activation in cycloheximide-treated Sp2/O-Ag14 cells, indicating that this antioxidant interferes with the apoptotic machinery. Our results indicate that some cell types are acutely sensitive to the toxic effect of ebselen, and that ebselen-induced cell death interferes with apoptotic processes. These observations are of particular importance since ebselen is currently used in clinical trials for possible use as therapeutic agent for stroke.
Acetylcysteine↗
Electron and atomic force microscopic investigations of lead selenide crystals grown under monolayers.
Lead selenide (PbSe) particulate films, composed of highly oriented, equilateral triangular crystals, have been in situ generated by the exposure of arachidic-acid- (AA) monolayer-coated aqueous lead nitrate [Pb(NO32] solutions to hydrogen selenide (H2Se). The AA coated PbSe films, at different stages of their growth, were transferred to solid substrates and characterized by transmission electron microscopy (TEM), electron diffraction, and atomic force microscopy (AFM). The epitaxial growth of PbSe crystals has been rationalized in terms of matching the [111] plane of crystalline PbSe and the (100) plane of the hexagonally close-packed AA monolayer. The parallel alignment of the < or = 110 > and < or = 001 > axes and the perpendicular alignment of the < or = 110 > axis to the monolayer have been suggested to be responsible for the observed formation of rod-like PbSe particles. The presence of a negatively charged monolayer has been found to be an essential requirement for the oriented growth of PbSe crystals.
Crystallization↗
Carbon dioxide laser skin resurfacing with a cooled handpiece.
BACKGROUND AND OBJECTIVE: Carbon dioxide (CO(2)) laser skin resurfacing has become an accepted procedure for the rejuvenation of aged and wrinkled facial skin. The benefits of this technique have been limited by the prolonged postoperative erythema, delayed re-epithelialization, and potential changes in pigmentation. We investigated the effects of coupling a pulsed CO(2) laser to a zinc selenide handpiece at various temperatures to cool and conduct heat from the skin surface. We compared the heat conducting handpiece to standard techniques used to determine the effects on epithelial preservation, depth of thermal damage, and new collagen growth. STUDY DESIGN/MATERIALS AND METHODS: The dorsal aspect of piglets was treated with four handpiece arrangements: no thermally conducting window; a zinc selenide thermally conducting window at room temperature; and the zinc selenide thermally conducting window cooled to 10 and 5 degrees C. Intensities were measured to account for reflections from the surface of the handpiece. With the CO(2) laser in scanning mode and a spot size of 1 mm, each handpiece was used at intensities ranging from 8-30 W in one pass. Biopsies for histopathologic analysis and determination of the degree of epithelial damage and the depth of thermal damage were taken on days 0, 2, and 16. RESULTS: All specimens revealed complete re-epithelialization by day 16. The addition of a cooled handpiece did not affect either the amount of epithelial preservation or the depth of thermal damage. CONCLUSIONS: There is no significant advantage in using a cooled or room temperature zinc selenide handpiece for epithelial preservation or decreasing the inflammatory response in CO(2) laser resurfacing.
Analysis of Variance↗
Refinement of the structure of human basic fibroblast growth factor at 1.6 A resolution and analysis of presumed heparin binding sites by selenate substitution.
The three-dimensional structure of human basic fibroblast growth factor has been refined to a crystallographic residual of 16.1% at 1.6 A resolution. The structure has a Kunitz-type fold and is composed of 12 antiparallel beta-strands, 6 of which form a beta-barrel. One bound sulfate ion has been identified in the model, hydrogen bonded to the side chains of Asn 27, Arg 120, and Lys 125. The side chain of Arg 120 has two conformations, both of which permit hydrogen bonds to the sulfate. This sulfate binding site has been suggested as the binding site for heparin (Eriksson, A.E., Cousens, L.S., Weaver, L.H., & Matthews, B.W., 1991, Proc. Natl. Acad. Sci. USA 88, 3441-3445). Two beta-mercaptoethanol (BME) molecules are also included in the model, each forming a disulfide bond to the S gamma atoms of Cys 69 and Cys 92, respectively. The side chain of Cys 92 has two conformations of which only one can bind BME. Therefore the BME molecule is half occupied at this site. The locations of possible sulfate binding sites on the protein were examined by replacing the ammonium sulfate in the crystallization medium with ammonium selenate. Diffraction data were measured to 2.2 A resolution and the structure refined to an R-factor of 13.8%. The binding of the more electron-dense selenate ion was identified at two positions. One position was identical to the sulfate binding site identified previously. The second selenate binding site, which is of lower occupancy, is situated 5.6 A from the first. This ion is hydrogen bonded by the side chain of Lys 135 and Arg 120. Thus the side chain of Arg 120 binds two selenate ions simultaneously. It is suggested that the observed second selenate binding site should also be considered as a possible binding site for heparin, or that both selenate binding sites might simultaneously contribute to the binding of heparin.
Amino Acid Sequence↗