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PubMed1995

The recharacterization of a polysaccharide iron complex (Niferex).

An oral hematinic marketed as "Niferex," the active component of which is a polysaccharide-iron complex (PIC), has recently been recharacterized. PIC is synthesized by the neutralization of an FeCl3 carbohydrate solution. Original characterization of this complex by Mössbauer spectroscopy and X-ray powder diffraction suggested that the iron-rich core was similar in structure to the mineral ferrihydrite. Higher precision X-ray powder diffraction now indicates that the core has a long-range order more similar to the mineral akaganéite, beta-FeOOH, than to ferrihydrite. This structure has been found for other similar ferric iron-carbohydrate polymers, especially those synthesized by the hydrolysis of FeCl3. Also discussed are the variable temperature (24-295 K) Mössbauer spectroscopic data for PIC. The first example of EXAFS data for polysaccharide iron complexes confirms that the iron is in an octahedral environment, coordinated to oxygen, with a short-range order similar to that for ferritin. The second iron shells in the PIC samples are less ordered than the second shell in ferritin. The size of the PIC core was found to be approximately 5 nm by X-ray powder diffraction, and is of the same order of magnitude as the ferritin core.

Iron↗

PubMed1995

A Mössbauer and X-ray powder diffraction study of some ferrous hematinics.

Iron deficiency anemia is a relatively common illness that can arise from a number of different causes. Three ferrous salts are usually used in its treatment: ferrous fumarate, gluconate, and sulfate. They are administered orally and are relatively well tolerated. These hematinics have been studied by Mössbauer spectroscopy and X-ray powder diffraction, and can easily be distinguished by both techniques. It was found that the two ferrous sulfates studied (Eckerd and SmithKline Beckman Co.) most closely resemble the monohydrate by comparison of the X-ray powder pattern with those of the JCPDS. Both the ferrous fumarate (Femiron) and gluconate (Spring Valley) had approximately 10% ferric iron present. To the authors' knowledge, this is the first reported Mössbauer spectrum for ferrous fumarate.

Ferrous Compounds↗

PubMed1994

Comparison of human oxyhemoglobin in lyophilized form, red blood cells, and concentrated solution: the features of Mössbauer spectra and heme iron stereochemistry.

Mössbauer spectra of human oxyhemoglobin in red blood cells, concentrated solution, and lyophilized form were measured at 87 K. Additionally, Mössbauer spectra of lyophilized oxyhemoglobin were measured at 295 K. The values of quadrupole splitting appeared to be the same for oxyhemoglobin in red blood cells and concentrated solution and slightly lower than those of oxyhemoglobin in lyophilized form. The asymmetry of the Mössbauer absorption line shapes previously observed for oxyhemoglobin in red blood cells was also found for oxyhemoglobin in concentrated solution. These Mössbauer spectra were better fitted using two quadrupole split doublets with almost equal areas. In contrast, Mössbauer spectra of lyophilized oxyhemoglobin were symmetrical and satisfactorily fitted with one quadrupole split doublet. However, these spectra were also fitted with two quadrupole split doublets with equal areas. The variations of the absorption line shapes and parameters of oxyhemoglobin Mössbauer spectra were analyzed in terms of stereochemical differences of the heme iron and Fe(II)-O2 bond in alpha- and beta-subunits of tetrameric oxyhemoglobin.

Erythrocytes↗

PubMed1996

The iron environment in heme and heme-antimalarial complexes of pharmacological interest.

Mössbauer spectroscopy has been utilized to probe the electronic environment of iron in a number of Ferriprotoporphyrin IX complexes of relevance to malaria. The markedly different iron environments found for the complexes of hemin with quinine, chloroquine, and the Chinese herbal antimalarial artesunate suggest that these compounds act by protecting the heme from polymerization to insoluble hemozoin, and by facilitating the transport of the protected heme to the food vacuole membrane where it is able to exercise its cytotoxic redox catalytic activity. Mössbauer parameters determined here for purified malaria pigment and synthetic beta-hematin confirm the chemical identical-ness of these species. The Mössbauer spectra of the complexes are discussed in light of the proposed structures of the complexes.

Animals↗

PubMed1988

Mössbauer spectroscopy, electron microscopy and electron diffraction studies of the iron cores in various human and animal haemosiderins.

Mössbauer spectroscopy has indicated significant differences in the iron-containing cores of various haemosiderins. In the present study, haemosiderin was isolated from a number of animal species including man. In addition, haemosiderin was isolated from patients with primary idiopathic haemochromatosis or with secondary (transfusional) iron-overload. The iron cores of the animal and normal human haemosiderin appear to be very similar by Mössbauer spectroscopy, and the electron diffraction data indicate a ferrihydrite structure similar to that of ferritin cores. The haemosiderin isolated from secondary iron-overload shows anomalous behaviour in its temperature-dependent Mössbauer spectra. This can be understood in terms of the microcrystalline goethite structure of the cores as indicated by electron diffraction. The haemosiderin cores obtained in the case of primary haemochromatosis have an amorphous Fe(III) oxide structure and show Mössbauer spectra characteristic of a magnetically disordered material, which only orders at very low temperatures.

Animals↗

PubMed1991

Mössbauer spectroscopic investigation of structure-function relations in ferritins.

Ferritin plays an important role in iron metabolism and our aim is to understand the mechanisms by which iron is sequestered within its protein shell as the mineral ferrihydrite. We present Mössbauer spectroscopic data on recombinant human and horse spleen ferritin from which we draw the following conclusions: (1) that apoferritin catalyses Fe(II) oxidation as a first step in ferrihydrite deposition, (2) that the catalysis of Fe(II) oxidation is associated with residues situated within H chains, at the postulated 'ferroxidase centre' and not in the 3-fold inter-subunit channels previously suggested as the initial Fe(II) binding and oxidation site; (3) that both isolated Fe(III) and Fe(III) mu-oxo-bridged dimers found previously by Mössbauer spectroscopy to be intermediates in iron-core formation in horse spleen ferritin, are located on H chains; and (4) that these dimers form at ferroxidase centres. The importance of the ferroxidase centre is suggested by the conservation of its ligands in many ferritins from vertebrates, invertebrates and plants. Nevertheless iron-core formation does occur in those ferritins that lack ferroxidase centres even though the initial Fe(II) oxidation is relatively slow. We compare the early stages of core formation in such variants and in horse spleen ferritin in which only 10-15% of its chains are of the H type. We discuss our findings in relation to the physiological role of isoferritins in iron storage processes.

Animals↗

PubMed1993

Structure and composition of ferritin cores from pea seed (Pisum sativum).

Iron cores from native pea seed (Pisum sativum) ferritin have been analysed by electron microscopy and Mössbauer spectroscopy and shown to be amorphous. This correlates with their relatively high phosphate content (Fe: P = 2.83; 1800 Fe, 640 P atoms/molecule). Reconstituted cores obtained by adding iron (2000 Fe atoms/molecule) in the absence of phosphate to pea seed apoferritin were crystalline ferrihydrite. In vitro rates of formation of pea-seed ferritin iron cores were intermediate between those of recombinant human H-chain and horse spleen apoferritin and this may reflect the amino-acid residues of its ferroxidase and putative nucleation centres. The high phosphate content of pea-seed ferritin suggests that this molecule could be involved in both phosphorus and iron storage. The high phosphate concentration found within plastids, from which the molecules were isolated, is a possible source of the ferritin phosphate.

Fabaceae↗

PubMed1992

A low-spin iron complex in human melanoma and rat hepatoma cells and a high-spin iron(II) complex in rat hepatoma cells.

Human melanoma and rat hepatoma cells cultured in the presence of low concentrations (2.5 microM) of low-molecular-weight iron (Fe) chelates and Fe-transferrin complexes have been studied with 57Fe Mössbauer spectroscopy. The spectra show that holoferritin is only a minor fraction of the total iron present in the cells. The major form of Fe was in a low-spin state unlike the high-spin Fe(III) found in ferritin. Only about 10% of the Fe could be attributed to ferritin. In addition, the hepatoma cells had a high-spin Fe(II) spectral component which made up about 20% of the Fe present.

Animals↗

PubMed1989

Mössbauer, EPR and NMR studies of the acid-induced reduction and changes in spin state of ferric bleomycin.

Iron-57 Mössbauer, electron paramagnetic resonance (EPR) and H-1 nuclear magnetic resonance (NMR) studies of iron-bleomycin complexes in the pH range from 1.0 to 6.0 are reported. Sequential protonation of the ligands produces a variety of high-spin and low-spin complexes of the metal. Of particular interest is the reversible equilibrium between Fe(III)- and oxygen-stable Fe(II)-bleomycin. Below pH 3.5 Fe(II) complexes form, with maximal reduction occurring at approximately pH 2. At still lower pH, Fe(III) complexes unassociated with bleomycin become dominant. The observed reduction in the absence of exogenous reducing agents suggests the possible involvement of intramolecular autoreduction in bleomycin-mediated DNA degradation.

Bleomycin↗

PubMed1995

Mixed valence state in ironporphyrin aggregates.

In biological systems, metalloporphyrins play a central role in energy and electron transfer process. Our aim is to understand the influence of ligands and iron coordination of ironporphyrin on the electron transfer. The lyophilized ironporphyrin, enriched in 57Fe up to 90% has been studied by Mössbauer spectroscopy between 2.8 and 313 K. Above room temperature the bounded diffusion of the ferric iron was observed. Below 293 K a part of iron appears in mixed Fe+3<==>Fe+2 valence state with 10 meV activation energy for the electron trapping. Below 4 K a part of iron shows magnetic ordering with a broad distribution of the hyperfine field. The results are discussed in terms of metalloporphyrin aggregation process.

Electrochemistry↗

PubMed1989

Mechanics of a single-ossicle ear: I. The extra-stapedius of the pigeon.

The motion of the conical peak of the tympanic membrane (TM) at the tip of the extra-stapedius (ES) and of the columella footplate (CFP) were measured in the pigeon using the Mössbauer technique. The dimensions of middle-ear structures were measured in some of the experimental animals. The averaged velocity response at the ES for frequencies of 0.25-2.378 kHz was that of a second order, mass and stiffness controlled, resonant system with resonant frequency of 1.2 kHz and Q3 dB of 1.2. The mean velocity amplitude at resonance was 3.7 mms-1 at 100 dB SPL, which is approximately equal to the theoretical value of 3.5 mms-1 required for maximum energy transfer from a uniform plane acoustic wavefront in air. For the frequency regions 0.125-0.25 kHz and 2.378-5.657 kHz, the mean amplitude slopes for the velocity at the ES were 2 dB oct-1 and -3 dB oct-1, respectively. Above 5.657 kHz there was considerable inter-animal variation in the ES velocity responses. The direction of motion at the ES was frequency dependent above 1 kHz. For frequencies up to 1 kHz the ratio of CFP to ES velocity was independent of frequency; the mechanical lever ratio was 2.7, which was attributed to the geometry of the middle ear. At these frequencies the total transformer ratio for the middle ear, expressing the ratio of fluid pressure at the CFP to sound pressure at the ES, was estimated to be 35 dB.

Acoustic Stimulation↗

PubMed1989

Mechanics of a single-ossicle ear: II. The columella footplate of the pigeon.

The motion of the columella footplate (CFP) was measured in the pigeon using the Mössbauer technique. At the upper frequency limit of the cochlea the measured CFP response exhibited anti-resonant phenomena. These high-frequency responses were dependent on the orientation of the radiation detector, in a way which could not be explained by the cosine effect. The dependence of the recorded phase response on the measurement axis implies an additional vibration mode, which was out of temporal phase and non-colinear with the presumed translational vibration mode. The anti-resonant phenomena were not observed when the cochlear labyrinth was extirpated, thus excluding an explanation in terms of extraneous vibrations in the experimental apparatus or of loading by the Mössbauer source. Intra-cochlear reflection is proposed as the origin of the interference mode.

Acoustic Stimulation↗

PubMed1991

Application of a commercially-manufactured Doppler-shift laser velocimeter to the measurement of basilar-membrane vibration.

A commercially-available laser Doppler-shift velocimeter has been coupled to a compound microscope equipped with ultra-long-working-distance objectives for the purpose of measuring basilar membrane vibrations in the chinchilla. The animal preparation is nearly identical to that used in our laboratory for similar measurements using the Mössbauer technique. The vibrometer head is mounted on the third tube of the microscope's trinocular head and its laser beam is focused on high-refractive-index glass microbeads (10-30 microns) previously dropped, through the perilymph of scala tympani, on the basilar membrane. For equal sampling times, overall sensitivity of the laser velocimetry system is at least one order of magnitude greater than usually attained using the Mössbauer technique. However, the most important advantage of laser-velocimetry vis-à-vis the Mössbauer technique is its linearity, which permits undistorted recording of signals over a wide velocity range. Thus, for example, we have measured basilar-membrane responses to clicks whose waveforms have dynamic ranges exceeding 60 dB.

Acoustic Stimulation↗

PubMed1995

Physical and chemical properties of superparamagnetic iron oxide MR contrast agents: ferumoxides, ferumoxtran, ferumoxsil.

The bulk physiochemical properties of the active ingredients in three AMI colloidal, superparamagnetic iron oxide (SPIO), MR contrast agents are described. Ferrous content and X-Ray diffraction (XRD) of the colloids are consistent with nonstoichiometric magnetite phases in all three active ingredients. No separate maghemite (gamma-Fe2O3) phases were detected by XRD. XRD line-broadening determinations of representative samples of ferumoxides (dextran coated), Ferumoxtran (dextran covered), and ferumoxsil (siloxane coated) yielded mean crystal diameters (volume weighted distribution) of 4.8-5.6, 5.8-6.2, and 7.9-8.8 nm, respectively. Transmission electron microscopy (TEM) showed that the crystal sizes were lognormally distributed with respective mean crystal diameters (number weighted distribution) of 4.3-4.8, 4.3-4.9, and 8.0-9.5 nm, respectively. Consistent with their small crystal sizes, the three SPIO colloids are superparamagnetic with no remanence after saturation at high applied fields (< 1 T), and showed characteristic relaxed Mössbauer spectra. The Mössbauer spectra of ferumoxides and Ferumoxtran were consistent with the presence of superparamagnetic relaxation above a blocking temperature of approximately 60 K. Due to the larger crystal sizes of ferumoxsil, its Mössbauer spectra showed the presence of rapid collective magnetic excitations on the Mössbauer time scale (approximately 1-10 ns). All three colloids showed high MR relaxivities. TEM of the SPIO colloids showed that ferumoxides and ferumoxsil are composed of aggregates of nonstoichiometric magnetite crystals, while Ferumoxtran consists of single crystals of nonstoichiometric magnetite. Dynamic light scattering (PCS) measurements showed that Ferumoxtran particles have average hydrodynamic diameters of approximately 21 nm (number weighted distribution) or 30 nm (volume weighted distribution). The data indicate that Ferumoxtran crystals are coated with an 8-12 nm layer of dextran T-10. Ferumoxides aggregates have average particle sizes of approximately 35 nm (number average distribution; TEM and PCS), or approximately 50 nm (volume weighted distribution; PCS). Mean sizes of ferumoxsil aggregates are approximately 300 nm (intensity weighted distribution). A discussion of the various particle size distributions is presented.

Chemical Phenomena↗

PubMed2004

Mössbauer spectroscopy and ELISA studies reveal differences between Parkinson's disease and control substantia nigra.

The possible role of iron in the degeneration of nervous cells in Parkinson's disease (PD) was studied with the use of Mössbauer spectroscopy (MS) and enzyme-linked immunoabsorbent assay (ELISA). Mössbauer data were obtained at 90 and 4.1 K from 21 samples of control and 9 samples of parkinsonian substantia nigra (SN). Mössbauer spectra were very similar to those observed in ferritin. Small differences were detected between the spectra obtained from PD and from control SN, and could be due to a slight difference in the composition of the ferritin-like iron cores or due to the presence of about 8% of non-ferritin-like iron in parkinsonian SN. ELISA studies from 11 controls and 6 parkinsonian SN showed a decrease in the concentration of L-chains in wet tissues of PD-SN compared to control SN. The decrease in the amount of L subunits may correspond to a decreased ability of this ferritin to keep iron in a safe form. Iron released from ferritin or neuromelanin (NM) may be the source of such iron, which may cause the difference in the Mössbauer spectra and may trigger oxidative stress leading to cell death.

Aged↗

PubMed2006

Characterization of complexes formed between [Me2Sn(IV)]2+ and carboxymethylcelluloses.

Complexes formed between carboxymethylcellulose (CMC) and the [Me(2)Sn(IV)]2+ cation have been prepared in the solid state and characterized by FTIR and Mössbauer spectroscopy. The complexes contained CMC with varying molar weight and degree of carboxylation, and the complexes were isolated both from acidic and from neutral solutions at varying metal-to-ligand ratios. The characteristic vibration bands of the ligands were identified from their pH-dependent FTIR spectra. In the organotin(IV) complexes obtained at pH approximately 2, the -COO- moieties were found to be coordinated in a monodentate manner, and the band characteristic of the protonated (unbound) -COO- group(s) was also identified. The broad -OH band can be interpreted as the sum of the contributions of the alcoholic -OH groups of the anhydroglucose units and the mixed organotin aqua complexes. In complexes obtained at pH approximately 7, the broad -OH band significantly sharpens, which is probably due to the metal-ion induced deprotonation and subsequent coordination of the alcoholic -OH groups. At the same time, -COO- groups are also involved in the coordination of the metal ions, resulting in a complicated network that forms through inter- and intramolecular bridges. Quadrupole splitting (/Delta(exp)/) values observed by Mössbauer spectroscopy revealed that the valence state of tin is four in all of the complexes. The /Delta(exp)/ values were compared with the calculated ones, obtained from the pqs theory. From these data, trigonal bipyramidal (Tbp) and octahedral (Oh) geometries have been suggested for the complexes obtained. It has also been concluded that the structure of the complexes prepared depends mainly on the pH of the solution, and it is relatively insensitive to the other parameters, like molar mass or degree of carboxylation of the ligand, or the metal-to-ligand ratio in the reaction mixture.

Carboxymethylcellulose Sodium↗

PubMed2006

Iron-oxide-modified nanosized diamond: preparation, characterization, and catalytic properties in methanol decomposition.

Nanosized diamond (UDD), obtained by a detonation procedure, was modified with iron from the corresponding acetylacetonate precursor under various pretreatment conditions. Nitrogen physisorption, X-ray diffraction, temperature-programmed reduction, and FTIR and Mössbauer spectroscopy were used for their characterization. The samples' catalytic behavior in methanol decomposition was also studied. The physicochemical and catalytic properties of the obtained materials (Fe/UDD) were compared with those of other iron-oxide-modified mesoporous supports with different nature and functionality (MCM-48 silica and CMK-1 carbon). The highest catalytic activity and stability was achieved with air-pretreated Fe/UDD.

Adsorption↗

PubMed2006

Chemical, physical, structural and morphological characterization of the electric arc furnace dust.

Electric arc furnace dust (EAFD) is a hazardous industrial waste generated in the collection of particulate material during steelmaking process via electric arc furnace. Important elements to the industry such as, Fe and Zn are the main ones in EAFD. Due to their presence, it becomes very important to know how these elements are combined before studying new technologies for its processing. The aim of this work was to carry out a chemical, physical, structural and morphological characterization of the EAFD. The investigation was carried out by using granulometry analysis, chemical analysis, scanning electron microscopy (SEM), energy dispersive spectroscopy via SEM (EDS), X-ray mapping analysis via SEM, X-ray diffraction (XRD) and Mössbauer spectroscopy. By XRD the following phases were detected: ZnFe(2)O(4), Fe(3)O(4), MgFe(2)O(4), FeCr(2)O (4), Ca(0.15)Fe(2.85)O(4), MgO, Mn(3)O(4), SiO(2) and ZnO. On the other hand, the phases detected by Mössbauer spectroscopy were: ZnFe(2)O(4), Fe(3)O(4), Ca(0.15)Fe(2.85)O(4) and FeCr(2)O(4). Magnesium ferrite (MgFe(2)O(4)), observed in the XRD pattern as overlapped peaks, was not identified in the Mössbauer spectroscopy analysis.

Brazil↗