Showing papers on "Ferric published in 1991"

Dinitrogen photoreduction to ammonia over titanium dioxide powders doped with ferric ions

Abstract: The production of ammonia from dinitrogen and water vapor at mild conditions of temperature and pressure on Fe{sup 3+}-doped titanium dioxide powders under UV radiation has been studied in a continuous photoreactor working in the gas-solid regime. A net activity decline was observed after a few hours of irradiation; this decline did not depend on the reactor temperature, the powder composition, or the amounts of produced ammonia. The highest activity is found when no excess iron is segregated at the surface; overall turnover numbers for dinitrogen reduction as high as six electrons per iron atom can then be reached before powder deactivation, showing the catalytic character of the participation of Fe in this process. An IR investigation of the active and spent specimens revealed that the irradiation determines the almost complete disappearance of the OH groups from the powder surface. Furthermore, an ESR study of all the powders showed that bulk Fe{sup 3+} ions are better electron traps than Ti{sup 4+} ions so that, when a UV photon generates a hole-electron pair, the electron can be stabilized on the iron ions.

Evaluation of ferrous and ferric Mössbauer fractions

Abstract: The Mossbauer fractions f for various ferrous- and/or ferric-containing oxides and oxyhydroxides, silicates and carbonates were evaluated from the experimental temperature dependence of their center shifts, using the Debye approximation for the second-order Doppler shift. It is concluded that ferrous ions exhibit a lower fraction as compared to ferric ions. Using standard mixtures of α-Fe2O3 with selected Fe2+ or Fe3+ compounds, it is found that the calculated Fe3+ f values are somewhat overestimated with respect to those of Fe2+. Possible explanations for this shortcoming are discussed and it is suggested that a different temperature dependence of the intrinsic isomer shift is the most likely reason. This suggestion is corroborated by analyses of hematite and hedenbergite data which are available for temperatures up to 900 K and 800 K respectively.

Ferric iron reduction by acidophilic heterotrophic bacteria.

Abstract: Fifty mesophilic and five moderately thermophilic strains of acidophilic heterotrophic bacteria were tested for the ability to reduce ferric iron in liquid and solid media under aerobic conditions; about 40% of the mesophiles (but none of the moderate thermophiles) displayed at least some capacity to reduce iron. Both rates and extents of ferric iron reduction were highly strain dependent. No acidophilic heterotroph reduced nitrate or sulfate, and (limited) reduction of manganese(IV) was noted in only one strain (Acidiphilium facilis), an acidophile which did not reduce iron. Insoluble forms of ferric iron, both amorphous and crystalline, were reduced, as well as soluble iron. There was evidence that, in at least some acidophilic heterotrophs, iron reduction was enzymically mediated and that ferric iron could act as a terminal electron acceptor. In anaerobically incubated cultures, bacterial biomass increased with increasing concentrations of ferric but not ferrous iron. Mixed cultures of Thiobacillus ferrooxidans or Leptospirillum ferrooxidans and an acidophilic heterotroph (SJH) produced sequences of iron cycling in ferrous iron-glucose media.

Roles of porphyrins and host iron transport proteins in regulation of growth of Porphyromonas gingivalis W50.

Abstract: Porphyromonas gingivalis (Bacteroides gingivalis) requires iron in the form of hemin for growth and virulence in vitro, but the contributions of the porphyrin ring structure, porphyrin-associated iron, host hemin-sequestering molecules, and host iron-withholding proteins to its survival are unknown. Therefore, the effects of various porphyrins, host iron transport proteins, and inorganic iron sources on the growth of P. gingivalis W50 were examined to delineate the various types of iron molecules used for cellular metabolism. Cell envelope-associated hemin and iron stores contributed to the growth of P. gingivalis in hemin-free culture, and depletion of these endogenous reserves required eight serial transfers into hemin-free medium for total suppression of growth. Comparable growth of P. gingivalis was observed with 7.7 microM equivalents of hemin as hemoglobin (HGB), methemoglobin, myoglobin, hemin-saturated serum albumin, lactoperoxidase, cytochrome c, and catalase. Unrestricted growth was recorded in the presence of haptoglobin-HGB and hemopexin-hemin complexes, indicating that these host defense proteins do not sequester HGB and hemin from P. gingivalis. The iron chelator 2,2'-bipyridyl functionally chelated hemin-associated iron, resulting in dose-dependent inhibition of growth in hemin-restricted cultures at 1 to 25 microM 2,2'-bipyridyl concentrations. In the absence of an exogenous iron source, protoporphyrin IX did not support P. gingivalis growth. These findings suggest that the iron atom in the hemin molecule is the critical constituent for growth and that the tetrapyrrole porphyrin ring structure may represent an important vehicle for delivery of iron into the P. gingivalis cell. P. gingivalis does not have a strict requirement for porphyrins, since growth occurred with nonhemin iron sources, including high concentrations (200 muM) of ferric, ferrous, and nitrogenous inorganic iron, and P. gingivalis exhibited unrestricted growth in the presence of host transferrin, lactoferrin, and serum albumin. The diversity of iron substrates utilized by P. gingivalis and the observation that growth was not affected by the bacteriostatic effects of host iron-withholding proteins, which it may encounter in the periodontal pocket, may explain why P. gingivalis is such a formidable pathogen in the periodontal disease process.

Empirical ferric iron corrections: necessity, assumptions, and effects on selected geothermobarometers

Abstract: The ferromagnesian silicate minerals, such as garnets, pyroxenes, micas, and amphiboles, appear in a variety of geothermometers and geobarometers. Where complete chemical analyses are available and regardless of bulk composition (metamorphosed pelitic or mafic), the aforementioned minerals commonly contain ferric iron. In mineral analyses using the electron microprobe, ferric and ferrous iron are not distinguished, and all the iron is treated as FeO. In ferric Fe-bearing minerals, this treatment results in (1) low analytical sums and (2) excess cations in the mineral formulae. Assuming ideal stoichiometry (ideal formula cations and oxygens) allows direct ferric estimates in garnets and pyroxenes; amphiboles require additional assumptions concerning site occupancies, and, for micas, no acceptable constraint exists for a ferric estimate. Based on ferric iron determinations for some metamorphic ferromagnesian silicates, the proportion of ferric to total iron increases at higher Xug values. The influence of ferric estimates on T and P calculations depends on the model used and on the extent the ferric estimate alters the relative proportions of end-members. Several examples suggest that, in general, if ferric estimates (or determinations) are made, they should be made for all the relevant minerals.

Identification and characterization of a Saccharomyces cerevisiae gene (PAR1) conferring resistance to iron chelators.

Abstract: o-Phenanthroline (1,10-phenanthroline) is a chemical known to chelate iron and other transition metal ions. This compound was added to solid yeast media to reduce the concentration of biologically available iron. Other essential divalent cations, like Zn2+ or Cu2+, which could also be bound, were supplemented. Growth of wild-type yeast strains was totally inhibited at specific concentrations of the chelator. However, several cells containing plasmids of a multicopy vector genomic library of S. cerevisiae could be selected by growth on these media. All of the resistant clones carried a single additional gene, PAR1 on their multicopy plasmids. Plasmid-directed overexpression of PAR1 increased the resistance of transformants to o-phenanthroline and additionally conferred resistance to 1-nitroso-2-naphthol, an iron(III)-binding molecule with different coordinating ligands. By supplementing the o-phenanthroline-containing media with several different metal ions, it could be proved that the selection plates really caused a specific iron limitation. These observations clearly demonstrated that the overexpressed PAR1 gene enables the cell to compete with iron-chelating organic molecules. PAR1 null mutants, constructed by insertion of the LEU2 gene into the open reading frame, showed a remarkable phenotype: they did not grow on slightly alkaline buffered media (pH greater than 7) and became hypersensitive to oxidative stress by hydrogen peroxide. Of several heavy metal ions, such as Fe3+, Fe2+, Co2+, Ni2+, Cu2+ and Zn2+, tested for supplementation of the alkaline growth deficiency, only iron, either added in the ferrous or ferric form, was able to restore cellular growth. It can be concluded from the DNA sequence that PAR1 encodes a highly acidic protein of 650 residues with mostly hydrophilic character. Some interesting repetitive amino acid motifs, such as (Asp-Asn)4 or Cys-Ser-Glu, may act as metal-binding sites. The possible role of PAR1 is discussed.

Clinical and chemical interactions between iron preparations and ciprofloxacin.

Abstract: 1. The effect of ferrous sulphate (300 mg), ferrous gluconate (600 mg), and a combination tablet of iron (10 mg), magnesium (100 mg), zinc (15 mg), calcium (162 mg), copper (2 mg), and manganese (5 mg) (Centrum Forte) co-administration on ciprofloxacin bioavailability was tested in eight healthy subjects. 2. Peak serum ciprofloxacin concentrations and area under the curve (AUC) were significantly reduced when ciprofloxacin was administered with 300 mg ferrous sulphate (3.0 vs 2.0 mg l-1, P less than 0.05 and 12.3 vs 6.7 mg l-1 h, P less than 0.01, respectively). Reductions in peak ciprofloxacin concentrations and AUC also occurred when ciprofloxacin was ingested with 600 mg ferrous gluconate (1.3 mg l-1, P less than 0.01 and 4.1 mg l-1 h, P less than 0.01, respectively) and a Centrum Forte tablet (1.4 mg l-1, P less than 0.01 and 5.4 mg l-1 h, P less than 0.01, respectively). 3. When ferrous ion was mixed with ciprofloxacin, rapid spectral changes occurred (t1/2 = 1.9 min). Additional studies were consistent with oxidation of the ferrous form of iron to its ferric form, which is followed by rapid formation of a Fe(3+)-ciprofloxacin complex. Ciprofloxacin seems to bind to ferric ion in a ratio of 3:1 by interacting with the 4-keto and 3-carboxyl groups on ciprofloxacin. 4. The formation of a ferric ion-ciprofloxacin complex is probably the cause of the reduction in ciprofloxacin bioavailability in the presence of iron.

Ferric ion promoted photodecomposition of triazines

Abstract: The aqueous photodegradation rates of the triazines atrazine, ametryn, prometon, and prometryn were greatly enhanced by the addition of 20-300 μM amounts of ferric perchlorate or ferric sulfate. The hydroxyl radical, HO . , drived from the photoreaction of the complex Fe(OH) 2+ , is likely to be active reactant. Known quenchers of HO . as well as constituents of buffers expected to react with HO . diminished the rate of reaction. Furthermore, photodegradation products of the atrazine/ferric iron system were the same as those for a Fenton reaction (known to involve HO . ) (...)

Calorimetric studies of the binding of ferric ions to ovotransferrin and interactions between binding sites.

Abstract: Transferrins are two-domain proteins with a very strong site for iron binding located in each domain Using ultrasensitive titration calorimetry, the binding of ferric ion (chelated with a 2-fold molar excess of nitrilotriacetate) to the two sites of ovotransferrin was studied in detail as well as the binding to the single site in the N- and C-terminal half-molecules In the presence of excess bicarbonate ion, the binding occurs in two kinetic steps The fast process of contact binding is instantaneous with respect to instrument response time, is strongly exothermic for the N site and less so for the C site, and corresponds to binding of the chelated ferric ion The slower process of bicarbonate insertion with concomitant release of nitrilotriacetate occurs on a time scale of 2-20 min over the temperature range 7-37 degrees C and is endothermic for the N site and exothermic for the C site, with rates being significantly slower for insertion at the C site The delta H of binding is strongly temperature-dependent for both sites, arising from a large negative delta Cp of binding which probably indicates removal of hydrophobic groups from contact with water When bicarbonate ion is absent, only the fast process of contact binding is seen Each site within a half-molecule is qualitatively similar to the same site in intact ovotransferrin, although quantitative differences were detected It was shown that contact binding to ovotransferrin occurs reversibly with free exchange of Fe+3 between N and C sites, while the attachment to either site becomes essentially irreversible after bicarbonate insertion The strong preference for the first ferric ion to bind to the N site is shown to be due to its larger contact binding constant and the faster rate of bicarbonate insertion, relative to the C site, and is not due to stronger thermodynamic binding after bicarbonate insertion True equilibrium is achieved only over much longer periods of time In another series of experiments, direct binding studies were carried out between the two half-molecules under different states of ligation with Fe+3 in the presence of bicarbonate The results indicate that the two binding sites in ovotransferrin, separated by ca 40 A, are not independent of one another but communicate as a result of ligand-dependent changes in the heats and free energies of domain-domain interactions(ABSTRACT TRUNCATED AT 400 WORDS)

Acquisition of iron by Legionella pneumophila: role of iron reductase.

Abstract: Legionella pneumophila has been shown to survive and multiply in a variety of intracellular environments, including protozoa and human mononuclear phagocytes. However, the mechanism by which this organism acquires iron in the intracellular environment has not been studied. Since L. pneumophila does not produce siderophores, alternative methods of iron acquisition were investigated. Virulent strains of L. pneumophila were able to grow in media containing as little as 3 microM iron, whereas avirulent cells required a minimum of 13 microM iron for growth. Neither virulent nor avirulent cells were able to utilize 55Fe bound to transferrin. When incubated in the presence of 55Fe in the form of ferric chloride, both virulent and avirulent cells accumulated equal amounts of iron. The uptake of iron was energy dependent as indicated by inhibition of 55Fe uptake at 4 degrees C and preincubation of the cells with KCN. Treatment of virulent cells with pronase or trypsin had no effect on iron uptake. In contrast, pronase or trypsin treatment of avirulent cells resulted in increased uptake of iron. Iron reductase activity in both virulent and avirulent cells was demonstrated, with the highest specific activity associated with the periplasmic fraction. Maximum reductase activity of virulent cells occurred with NADH as the reductant. In contrast, avirulent cells showed a twofold increase in enzyme activity when NADPH was used as the reductant. These results suggest that an iron reductase is important in iron acquisition by L. pneumophila.

Ferrous iron dependent nitric oxide production in nitrate reducing cultures of Escherichia coli

Abstract: l-Lactate-driven ferric and nitrate reduction was studied in Escherichia coli E4. Ferric iron reduction activity in E. coli E4 was found to be constitutive. Contrary to nitrate, ferric iron could not be used as electron acceptor for growth. “Ferric iron reductase” activity of 9 nmol Fe2+ mg-1 protein min-1 could not be inhibited by inhibitors for the respiratory chain, like Rotenone, quinacrine, Actinomycin A, or potassium cyanide. Active cells and l-lactate-driven nitrate respiration in E. coli E4 leading to the production of nitrite, was reduced to about 20% of its maximum activity with 5 mM ferric iron, or to about 50% in presence of 5 mM ferrous iron. The inhibition was caused by nitric oxide formed by a purely chemical reduction of nitrite by ferrous iron. Nitric oxide was further chemically reduced by ferrous iron to nitrous oxide. With electron paramagnetic resonance spectroscopy, the presence of a free [Fe2+-NO] complex was shown. In presence of ferrous or ferric iron and l-lactate, nitrate was anaerobically converted to nitric oxide and nitrous oxide by the combined action of E. coli E4 and chemical reduction reactions (chemodenitrification).

Iron(III) coordination chemistry of linear dihydroxyserine compounds derived from enterobactin

Abstract: The solution thermodynamic stability and iron transport properties of the hydrolysis products of enterobactin are reported. Enterobactin, a tricatechol siderophore, is a cyclic trilactone that undergoes three stepwise hydrolysis reactions to form a linear trimer, then dimer, and finally the monomeric N-(2,3-dihydroxybenzoyl)serine. The protonation and ferric complex formation constants of the linear trimer and linear dimer have been determined. The enthalpies of formation of the linear trimer complex and ferric enterobactin have been measured by calorimetric titrations

Water-soluble ferric porphyrinates: solution and solid-state species.

Abstract: The nature of the aqueous solution axial ligands of the water-soluble iron (III) porphyrinates [Fe(TMPyP)] 5+ and [Fe(TPPS)] 3− has been examined as a function of pH by 1 H NMR spectroscopy

Inhibition of iron absorption by omeprazole in rat model

Abstract: Since gastric acid is an important luminal factor in the absorption of non-heme iron, the effect of omeprazole on the absorption of iron in a rat model was studied. Iron absorption studies were performed on rats on a normal diet (N=42) and rats fed an iron-deficient diet (N=43) for three weeks. Rats were orally dosed with 40 μmol/kg of omeprazole or placebo daily for two days prior to iron absorption studies. Rats were orally dosed with 1 mmol of ferrous chloride, ferric chloride or food iron (dietary suspension) containing 11 μg of iron and labeled with 1 μCi of59Fe. Omeprazole-treated rats on the normal diet had no significant reduction in the absorption of ferric, ferrous, or food iron. In the rats on the iron-deficient diet, the absorption of ferrous iron decreased from 76±7.5% (mean±se) in control rats to 38±8.5% in the omeprazole-treated rats (P<0.003) and the absorption of food iron decreased from 65±7.5% in control rats to 37±6.5% in the omeprazole-treated rats (P<0.016). There was no significant reduction in the absorption of ferric iron. Omeprazole therapy is unlikely to be associated with significant iron malabsorption in normal patients but may reduce iron absorption in pathological states associated with increased iron absorption such as iron deficiency.

Effects of citrate ions on the formation of ferric oxide hydroxide particles

Abstract: The effects of citrate ions on the formation of β- and α-FeOOH particles were investigated using various techniques. The formation and crystallization of both particles were inhibited by citrate ions, and their particle sizes decreased with increase in the concentration of these ions. Finally, aggregated amorphous particles were formed. The effects of citrate ions appeared to be more significant for β-FeOOH than for α-FeOOH. This difference could be explained by the pH dependence of the affinity of citrate ions to Fe3+ ions. The amorphous β-FeOOH particles prepared in the presence of > 10 mol% citrate ions selectively adsorbed water molecules.

Ferric-salicylaldehyde isonicotinoyl hydrazone, a synthetic iron chelate, alleviates defective iron utilization by reticulocytes of the Belgrade rat.

Abstract: The Belgrade rat has a hypochromic, microcytic anemia inherited as an autosomal recessive mutation. Although transferrin binds normally to reticulocytes and internalizes normally, iron accumulation into cells and heme is much slower than normal. We have investigated the role of the transferrin cycle in this mutant by bypassing transferrin iron delivery with the iron chelate ferric salicylaldehyde isonicotinoyl hydrazone (Fe-SIH). Fe-SIH increases iron uptake into heme by Belgrade reticulocytes, restoring it almost to normal levels. This increase indicates that Fe-SIH delivers iron to a step in iron utilization that is after the Belgrade defect. Depleting reticulocytes of transferrin did not alter these observations. Failure to achieve above normal rates of iron incorporation could indicate damage due to chronic intracellular iron deficiency. Also, iron delivery by Fe-SIH restored globin synthesis to near-normal levels in Belgrade reticulocytes. The rates of glycine incorporation into porphyrin and heme in Belgrade reticulocytes incubated with Fe2-transferrin or Fe-SIH paralleled the rates of iron incorporation into heme. These data are consistent with the concept that iron availability limits protoporphyrin formation in rat reticulocytes. The protoporphyrin used for heme synthesis is provided by de novo synthesis and not by a pool of pre-existing protoporphyrin. The Belgrade defect occurs in the movement of iron from transferrin to a step prior to reduction to the ferrous state and insertion into heme. This defect diminishes the synthesis of heme and, consequently, that of protoporphyrin and globin.