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PubMed2005

Chromate reduction and retention processes within arid subsurface environments.

Chromate is a widespread contaminantthat has deleterious impacts on human health, the mobility and toxicity of which are diminished by reduction to Cr(III). While biological and chemical reduction reactions of Cr(VI) are well resolved, reduction within natural sediments, particularly of arid environments, remains poorly described. Here, we examine chromate reduction within arid sediments from the Hanford, WA site, where Fe(III) (hydr)oxide and carbonate coatings limit mineral reactivity. Chromium(VI) reduction by Hanford sediments is negligible unless pretreated with acid; acidic pretreatment of packed mineral beds having a Cr(VI) feed solution results in Cr(III) associating with the minerals antigorite and lizardite in addition to magnetite and Fe(II)-bearing clay minerals. Highly alkaline conditions (pH > 14), representative of conditions near high-level nuclearwaste tanks, result in Fe(II) dissolution and concurrent Cr(VI) reduction. Additionally, Cr(III) and Cr(VI) are found associated with portlandite, suggesting a secondary mechanism for chromium retention at high pH. Thus, mineral reactivity is limited within this arid environment and appreciable reduction of Cr(VI) is restricted to highly alkaline conditions resulting near leaking radioactive waste disposal tanks.

Chromates↗
PubMed2006

Pollution of the Begej Canal sediment--metals, radioactivity and toxicity assessment.

The Begej Canal is one among a large number of canals in Vojvodina (Northern Province of Serbia and Montenegro). The paper describes a study of metal and radioactivity contamination of the Begej Canal sediment. It is also concerned with the evaluation of sediment acute toxicity based on standard test species Daphnia magna and simultaneously extracted metals and acid volatile sulfides. The quality of sediment was assessed according to Dutch standards, but the results were also compared with some Canadian and USEPA (United States Environmental Protection Agency) guidelines for sediment quality. The results showed severe pollution with chromium, copper, cadmium and zinc, whereby the anthropogenic origin of these contaminants was indicated. The tests of toxicity of sediment pore water to D. magna, gave no indication of the presence of substances in acutely toxic concentrations to this species. It can be speculated that, despite of high metal contents, the observed toxicity was low because of the high contents of clay and iron, as well as sulphide. Also, based on a comparison with the Danube sediment and Vojvodina soil in general, the data of the Begej sediment contamination with 238U and 137Cs. The 137Cs data were used for approximate dating of the sediment. No traces of contamination by nuclear power plants in the region were found, while the presence of technologically enhanced naturally occurring radioactive materials (TENORM) was proved. Conclusions based on different criteria for sediment quality assessment were in some cases contradictory. Study also showed that radioactivity aspects can be useful in sediment quality surveys. The obtained results will be invaluable for the future activities regarding integrated water management based on EC Water Framework Directive (2000/60/EC) in the Danube basin, and particularly in the region of crossborder water body of the Begej Canal.

Animals↗
PubMed1988

Ribonucleotide reductase of Brevibacterium ammoniagenes is a manganese enzyme.

Ribonucleotide reduction and not DNA replication is the site for the specific manganese requirement of DNA synthesis and cell growth in the coryneform bacterium Brevibacterium ammoniagenes. To characterize the metal effect we have isolated and purified ribonucleoside-diphosphate reductase from overproducing bacteria that were first deprived of and then reactivated by manganese ions. Purification on columns of Sephacryl S400, DEAE-cellulose and hydroxyapatite provided an apparently homogeneous enzyme consisting of two protein subunits. These were characterized by affinity chromatography on 2',5'-ADP-Sepharose as nucleotide-binding protein B1 (Mr = 80,000) and catalytic protein B2 (Mr = 100,000, composed of two Mr = 50,000 polypeptides), which were both necessary for activity. In vitro the purified enzyme does not require added metal ions except for an unspecific, twofold activity increase observed in the presence of Mg2+ and other divalent cations. Enzyme activity is inhibited by hydroxyurea (I50 = 2.5 mM). The electronic spectrum with maxima around 455 nm and 485 nm closely resembles that of manganese(III)-containing pseudocatalase and of oxo-bridged binuclear Mn(III) model complexes. Denaturation of the enzyme in trichloroacetic acid liberated an equimolar amount of Mn(II) which was detected by EPR spectroscopy. It was not possible to remove and reintroduce metal ions without loss of enzyme activity. Manganese-deficient cell cultures were also grown in the presence of 54MnCl2. Ribonucleotide reductase activity and radioactivity cochromatographed in several systems. Non-denaturing polyacrylamide gel electrophoresis showed that protein subunit B2 was specifically 54Mn-labeled. All these properties suggest that the ribonucleotide reductase of B. ammoniagenes is a manganese-containing analog of the non-heme-iron-containing reductases of Escherichia coli and eukaryotes.

Brevibacterium↗
PubMed2002

226Ra/238U disequilibrium in an upland organic soil exhibiting elevated natural radioactivity.

This paper presents the results of a study into the anomalous 226Ra/238U disequilibrium (226Ra/238U of 0.5-9) exhibited by an upland organic soil in Co. Donegal, Ireland. Radiochemical speciation of 226Ra, 238U and 225Ra indicates that in this organic soil the high 226Ra/238U ratio is due to loss of 235U relative to 226Ra via oxidation and mobilisation of 238U in the upper layers of the soil and subsequent loss in solution. At the lower, more reducing depths of the soil profile, 238U and 226Ra are essentially in equilibrium. Loss of 238U appears to occur primarily from the easily oxidised organic and iron oxide fractions of the soil, samples exhibiting high 226Ra/238U ratios displaying significantly lower 238U levels in these fractions than samples whose ratio is below the average value for the soil of the valley. Selective enrichment of 226Ra by plants or preferential leaching of 226Ra from the underlying rock is not supported by the results of this study.

Ferric Compounds↗
PubMed2001

Sorption behavior of U(VI) on phyllite: experiments and modeling.

The sorption of U(VI) onto low-grade metamorphic rock phyllite was modeled with the diffuse double layer model (DDLM) using the primary mineralogical constituents of phyllite, i.e. quartz, chlorite, muscovite, and albite, as input components, and as additional component, the poorly ordered Fe oxide hydroxide mineral, ferrihydrite. Ferrihydrite forms during the batch sorption experiment as a weathering product of chlorite. In this process, Fe(II), leached from the chlorite, oxidizes to Fe(III), hydrolyses and precipitates as ferrihydrite. The formation of ferrihydrite during the batch sorption experiment was identified by Mössbauer spectroscopy, showing a 2.8% increase of Fe(III) in the phyllite powder. The ferrihydrite was present as Fe nanoparticles or agglomerates with diameters ranging from 6 to 25 nm, with indications for even smaller particles. These Fe colloids were detected in centrifugation experiments of a ground phyllite suspension using various centrifugal forces. The basis for the successful interpretation of the experimental sorption data of uranyl(VI) on phyllite were: (1) the determination of surface complex formation constants of uranyl with quartz, chlorite, muscovite, albite, and ferrihydrite in individual batch sorption experiments, (2) the determination of surface acidity constants of quartz, chlorite, muscovite, and albite obtained from separate acid-base titration, (3) the determination of surface site densities of quartz, chlorite, muscovite, and albite evaluated independently of each other with adsorption isotherms, and (4) the quantification of the secondary phase ferrihydrite, which formed during the batch sorption experiments with phyllite. The surface complex formation constants and the protolysis constants were optimized by using the experimentally obtained data sets and the computer code FITEQL. Surface site densities were evaluated from adsorption isotherms at pH 6.5. The uranyl(VI) sorption onto phyllite was accurately modeled with these newly determined constants and parameters of the main mineralogical constituents of phyllite and the secondary mineralization phase ferrihydrite. The modeling indicated that uranyl sorption to ferrihydrite clearly dominates uranyl sorption, showing the great importance of secondary iron phases for sorption studies.

Adsorption↗
PubMed1977

Disposition in rats of the carbohydrate polymer in Ferastral--an iron-poly (sorbitol-gluconic acid) complex.

The disposition and pharmacokinetics in rats of 14C-sorbitol-Ferastral has been studied as an initial step towards elucidating the metabolic fate of the polymeric organic moiety. The period of time studied was 24 h. Following i.v. administration of a dose corresponding to 10 mg/kg of iron approximately 60% of the isotope was found in the urine after this period of time. A further 3% was demonstrated in the faeces whilst the expired air accounted for about 10% in the form of 14CO2. Thus, a relatively large proportion of the radiolabel was promptly excreted via the kidneys whilst the expired air and probably bile constituted secondary excretion routes. The physico-chemical nature of the urinary product was similar to the parent carbohydrate compound. The residual 14C radioactivity was distributed mainly between the liver, which contained approximately 45% of the retained label, carcass with 36% and large intestine with 7%. The plasma disappearance pattern was biphasic. Similar experiments with the 14C-sorbitol polymer starting material were performed for purposes of comparison.

Animals↗
PubMed1996

Tritrichomonas foetus: iron acquisition from lactoferrin and transferrin.

Acquisition of iron from lactoferrin and transferrin by a parasitic protozoon Tritrichomonas foetus has been studied in vitro. Specific, time-dependent, and saturable binding of iodinated ligands to the outer membrane of T. foetus at 4 degrees C was demonstrated for 125I-labeled lactoferrin only. About 1.7 x 10(5) binding sites of a single class with Kd approximately equal to 3.6 microM was estimated by means of Scatchard analysis. Internalization of the bound lactoferrin was observed at 37 degrees C. The cell-associated radioactivity after 30 min incubation of the parasite with 125I-lactoferrin at 37 degrees C was about 3.5-fold higher than the amount bound at 4 degrees C. The majority of internalized 125I-lactoferrin was released within 15 min of cell reincubation at 37 degrees C in the presence of a 100-fold excess of nonlabeled lactoferrin. Released lactoferrin displayed unchanged mobility on autoradiography. In contrast to lactoferrin, binding of 125I-transferrin was nonspecific and did not display saturable kinetics. The growth of T. foetus in iron-restricted media was stimulated by both lactoferrin and transferrin. The ability of the cells to remove and accumulate iron from both proteins was therefore examined using 59Fe-saturated lactoferrin and transferrin. It was found that trichomonads acquired a comparable amount of iron from both lactoferrin and transferrin during 60 min incubation at 37 degrees C (495 and 577 pmole Fe/mg of protein, respectively). The pH of the assay medium (PBS) decreased from pH 7.4 to 5.6 after incubation with trichomonads. At this pH, marked release of iron from transferrin (up to 47%) but not from lactoferrin (4%) was determined in cell-free media. These results indicate that T. foetus is able to utilize both lactoferrin and transferrin to cover its iron requirements. However, mechanisms of iron acquisition from these host proteins appear to be different. Specific binding and internalization of lactoferrin suggests the possible involvement of receptor-mediated endocytosis in the acquisition of lactoferrin-bound iron, while retrieval of iron from transferrin may depend on the extracellular release of iron from this ligand.

2,2'-Dipyridyl↗
PubMed1984

Incorporation of [35S]sulfide into the Fe-S cluster of aconitase.

Exchange of sulfide into the iron-sulfur cluster of beef heart aconitase was investigated using Na235S. After anaerobic incubation for minutes and up to 24 h, samples were freed of substances of low Mr by Sephadex G-50 and analyzed for protein, protein-bound Fe, S2-, total Fe-S cluster by EPR, and for radioactivity. The activated and the inactive enzyme exchange three S2- ions within 1-2 h at essentially equal rates. No further exchange is observed with the activated enzyme within 24 h, whereas with the inactive enzyme, (partial) exchange of one more S2- occurs slowly within 5-10 h. Exchange is facilitated at elevated pH, but then destruction of clusters also increases. During incubation of inactive enzyme with S2-, partial activation may occur because S2- can act as reductant. Thus, depending on conditions, we observed very low to substantial activities. There is a linear, positive correlation between activity developed and ratio of cluster bound Fe to S2-. When Fe and dithiothreitol are present together with S2- during incubation, the extent of S2-exchange generally is between 10 and 25%. Fe incorporation exceeds S2- exchange, with the difference between Fe and S2- incorporation consistently amounting to one Fe/cluster. It is suggested that this excess Fe represents the Fe ion taken up on completion of the [4Fe-4S] from the [3Fe-4S] structure. The ease of S2-exchange suggests that the Fe-S cluster of aconitase is readily accessible to solvent.

Aconitate Hydratase↗
PubMed1991

Identification of the NADH-binding subunit of energy-transducing NADH-quinone oxidoreductase (NDH-1) of thermus thermophilus HB-8.

The energy-transducing NADH--quinone oxidoreductase (NDH-1) isolated from Thermus thermophilus HB-8 is composed of approximately 10 unlike polypeptides and contains noncovalently bound FMN and at least three iron-sulfur clusters [Yagi, T., Hon-nami, K., and Ohnishi, T. (1988) Biochemistry 27, 2008-2013]. When NDH-1 of T. thermophilus HB-8 was irradiated by short UV light in the presence of [adenylate-32P]NADH or [adenylate-32P]NAD, radioactivity was incorporated into a single polypeptide of Mr 47,000. The labeling of the Mr 47,000 polypeptide was diminished when UV irradiation of the enzyme complex with [adenylate-32P]NAD was carried out in the presence of NADH or deamino-NADH which act as substrates for the NDH-1, but not in the presence of NADP(H) or AMP which act neither as substrates nor as competitive inhibitors. These results strongly suggest that the Mr 47,000 polypeptide is an NADH-binding subunit of the NDH-1 of T. thermophilus HB-8.

Adenosine Monophosphate↗
PubMed1987

Siderosomal ferritin. The missing link between ferritin and haemosiderin?

A minor electrophoretically fast component was found in ferritin from iron-loaded rat liver in addition to a major electrophoretically slow ferritin similar to that observed in control rats. The electrophoretically fast ferritin showed immunological identity with the slow component, but on electrophoresis in SDS it gave a peptide of 17.3 kDa, in contrast with the electrophoretically slow ferritin, which gave a major band corresponding to the L-subunit (20.7 kDa). Thus the electrophoretically fast ferritin resembles that reported by Massover [(1985) Biochim. Biophys. Acta 829, 377-386] in livers of mice with short-term parenteral iron overload. The electrophoretically fast ferritin had a lower iron content (2000 Fe atoms/molecule) than the electrophoretically slow ferritin (3000 Fe atoms/molecule). Removal and re-incorporation of iron was possible without effect on the electrophoretic mobility of either ferritin species. On subcellular fractionation the electrophoretically fast ferritin was enriched in pellet fractions and was the sole soluble ferritin isolated from iron-laden secondary lysosomes (siderosomes). The amount and relative proportion of the electrophoretically fast species increased with iron loading. Haemosiderin isolated from siderosomes was found to contain a peptide reactive to anti-ferritin serum and corresponding to the 17.3 kDa peptide of the electrophoretically fast ferritin species. Unlike the electrophoretically slow ferritin, the electrophoretically fast ferritin did not become significantly radioactive in a 1 h biosynthetic labelling experiment. We conclude that the minor ferritin is not, as has been suggested for mouse liver ferritin, 'a completely new species of smaller holoferritin that represents a shift in the ferritin phenotype' in response to siderosis, but a precursor of haemosiderin, in agreement with the proposal by Richter [(1984) Lab. Invest. 50, 26-35] concerning siderosomal ferritin.

Animals↗
PubMed1997

Improvement of the Eakins and Brown method for measuring 59Fe and 55Fe in blood and other iron-containing materials by liquid scintillation counting and sample preparation using microwave digestion and ion-exchange column purification of iron.

The simultaneous measurement of 59Fe and 55Fe in whole blood by liquid scintillation counting by the Eakins and Brown (EB) method is extensively used in iron absorption studies. The EB method requires many steps which increase the chances of error and decrease its sensitivity. We describe two modifications to the above method consisting of microwave digestion and column purification of iron. This "New Method" (NM) is simpler and more precise, and sensitive than the EB method. Counting efficiencies with the NM are similar for 59Fe (75%) as with the EB method but are better for 55Fe (29% for NM vs 22%), and cross counting from 59Fe into the 55Fe window is lower with the NM (3.7-4.5%) than with the EB method (10-12%). For the NM, recoveries of radioactive blood samples, in relation to processed standards ranged from 100 to 103% for 59Fe and 101 to 113% for 55Fe. For the EB method, recoveries ranged from 94 to 99% for 59Fe and from 88 to 93% for 55Fe. Even with very low counts, average intrarun CV with the NM was lower than 5.4% for either isotope, while it was as high as 10.0% for 55Fe with the EB method.

Animals↗
PubMed2003

Effect of immunoglobulin G from cows immunized with ferric citrate receptor (FecA) on iron uptake by Escherichia coli.

The effects of immunoglobulin (Ig) G from cows immunized with the ferric citrate receptor (FecA) on iron uptake by Escherichia coli were investigated. Receptor FecA was purified from E. coli UT5600/pSV66. Cows were immunized with 400 microg purified FecA three times at 21 d intervals during late lactation and the nonlactating period. Immunoglobulin G was purified by protein G affinity chromatography from colostral whey from cows immunized with FecA and from unimmunized control cows. The purified IgG from FecA immunized cows had higher IgG titers against FecA compared with control IgG. Fifteen E. coli isolated from intramammary infections and E. coli UT5600/pSV66 were grown in an iron-depleted medium containing 1 mM citrate to induce FecA. The bacterial cells were mixed with 0, 2, and 4 mg/ml purified IgG, and 55Fe was added to the assay. After 5, 10, and 15 min incubations at 37 degrees C, samples were passed through 0.45-pm pore size filters. Filters were washed with saline three times, and the radioactivity of 55Fe taken up by the bacterial cells on the filters was measured by a liquid scintillation counter. The measurements were expressed as numbers of 55Fe atoms per colony-forming unit and transformed to log10. The assay was repeated three times for each isolate in a partially balanced incomplete block design. The presence of IgG decreased 55Fe uptake by E. coli mastitis isolates and E. coli UT5600/pSV66. Anti-FecA IgG reduced 55Fe uptake by E. coli greater than IgG from unimmunized cows.

Animals↗
PubMed2002

About the assumption of linearity in soil-to-plant transfer factors for uranium and thorium isotopes and 226Ra.

The linearity assumption for soil and plant concentrations of radionuclides is usually a good approximation for use in food-chain models. To verify this assumption, different samples of plant and substrate were collected from a granitic zone located near a disused uranium mine in order to cover a large range of concentrations. In all of the samples, the activity concentration of 226Ra and of different isotopes of uranium (238U and 234U) and thorium (232Th, 230Th and 228Th) were determined. The results indicate that the linearity assumption can be considered valid when the range of concentrations taken into account is large (approx. two orders of magnitude). Otherwise, there is a clear deviation from linearity. Also, the influence of different stable elements on the soil-plant transfer factors was studied by using multivariate regression methods. The uptake of uranium, thorium and radium was found to be mainly associated with the concentration of iron in the plant and the phosphorus and alkaline earths in the substrate.

Food Chain↗
PubMed1994

[The electrolyte and trace element content of the blood in participants in the cleanup of the accident at the Chernobyl Atomic Electric Power Station].

Electrolyte equilibrium and microelemental composition of blood as well as mechanisms of their control were studied in remote period after patients exposure to complex influence of factors associated with radiation accident. The following regularity was observed: total level of electrolytes was decreased in plasma but increased in erythrocytes. These changes are caused by disorders of hormonal regulation. Dysbalance between oxidant and anti-oxidant systems, increased contents of lead, cobalt and iron in the blood may be a pathological basis for development of free radical pathology in examined patients.

Accidents, Occupational↗
PubMed1998

Caco-2 cell ferritin formation predicts nonradiolabeled food iron availability in an in vitro digestion/Caco-2 cell culture model.

We have adapted an in vitro digestion/Caco-2 cell model to assess Fe availability from foods, by using ferritin formation by Caco-2 cells as an indicator of Fe uptake. Ferritin formation by Caco-2 cells occurs in response to Fe uptake at concentrations of available Fe greater than that of the culture media to which the cells have been adapted. This methodology circumvents the need for using radioactive Fe and thus eliminates the costs and controversies associated with food radiolabeling. To validate this method, we measured ferritin formation in Caco-2 cells exposed to digests containing Fe of relatively high and low availability. Our objective was to determine if ferritin formation would be proportional to Fe uptake and sufficiently sensitive to be an indicator of Fe availability from food digests. Our model uses established in vitro digestion techniques coupled with uptake of Fe by Caco-2 cell monolayers. Measurement of cell ferritin was done by a commercially available RIA. Higher ferritin formation was observed in cells exposed to digests containing FeSO4 plus ascorbic acid vs, digests containing FeSO4 plus citric acid. Additional comparisons of Fe availability from digests of beef, fish, corn and green beans yielded results that demonstrate higher Fe availability (i.e., greater ferritin formation) from beef and fish digests than from digests of corn and green beans. Overall, the results document the promotional effects of ascorbic acid and animal tissue on Fe uptake as measured indirectly by ferritin formation. The results of this study indicate that ferritin formation by Caco-2 cell monolayers is highly sensitive and accurately measures food Fe availability in this in vitro system.

Caco-2 Cells↗