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PubMed1995

Inhibition of adenylyl cyclase in rat striatal homogenates by combinations of dopamine and ferric iron compounds.

The adenylyl cyclase activity of homogenates of striatal tissue from rat brain has been used as a model to test the hypothesis that the products of the reaction of polyphenols with ferric iron compounds are toxic. Dopamine (DA), at levels that stimulate adenylyl cyclase, inhibited the activity in the presence of 2 mol of potassium ferricyanide (FC), methemoglobin or ferricytochrome c per mol of DA. Combinations of potassium ferrocyanide and DA were not inhibitory. Neither pyrocatechol nor hydroquinone stimulated the activity, but these polyphenols were inhibitory in the presence of FC. Tyramine, phosphorylated DA or phosphorylated pyrocatechol had no effect on the activity of the enzyme in the presence or absence of FC. Forskolin was unable to stimulate the adenylyl cyclase once the latter was inhibited by DA plus FC, and dithiothreitol could not reverse inhibition by DA plus FC. Incubation of DA with FC, in the absence of the homogenate, resulted in substances that were not inhibitory. These findings suggest that the polyphenols plus FC react to yield substances that inhibit the adenylyl cyclase by affecting the catalytic unit of the enzyme complex.

3,4-Dihydroxyphenylacetic Acid↗
PubMed1981

Assmilation of iron by pathogenic Neisseria spp.

Iron assimilation by Neisseria meningitidis and Neisseria gonorrhoeae has been shown to be important to their growth and virulence. Iron acquisition in vitro was studied in an agar diffusion assay employing the iron-binding protein conalbumin. The ability of various iron compounds to alter the growth-inhibitory effect of conalbumin was investigated. On an equimolar iron basis, citrate-containing iron compounds were most effective; hemin was slightly less effective; ferrous sulfate and ferrous ammonium sulfate were even less effective; and the ferric compounds, ferric nitrate, ferric chloride, and ferric dextran (Imferon), were least effective. The results suggested that, as with Escherichia coli and certain other bacteria, the Neisseria spp. may utilize a citrate-mediated iron transport system. Microbial siderophores were also tested for their ability to relieve the growth-inhibitory effect of conalbumin. Two phenolate siderophores and Desferal enhanced growth inhibition in the deferrated form, but were inactive in the ferrated form. Several trihydroxamates of the ferrichrome family and coprogen were inactive in either the deferrated or ferrated forms. Of the 12 different siderophores tested, only the dihydroxamates (schizokinen, arthrobactin, and aerobactin) were stimulatory, but then only in the ferrated forms. Apparently, even though those siderophores could be utilized as specific iron transport agents by the Neisseria spp., they could not compete with conalbumin for iron under these assay conditions.

Conalbumin↗
PubMed1970

An analysis of the electron spin resonance of low spin ferric heme compounds.

The electron spin resonance spectra of low spin ferric heme proteins are calculated and compared with experimental spectra recently obtained for a large number of heme proteins. On the basis of observed g values, these heme proteins have been categorized into five prototypes. Since electron spin resonance spectra are quite sensitive to small changes in the local environment about the paramagnetic ion, we have explored in some detail, the possibility that the g value variation in these different types of proteins is due to systematic environmental changes. To this end, we have calculated the g values as a function of tetragonal and rhombic distortions and compared our results with observed behavior. In addition we have also calculated the energy intervals between the low spin states in zero magnetic field and the temperature dependent magnetic moments and studied the effect on these properties also of small symmetry changes.

Chemical Phenomena↗
PubMed2006

[Analysis of the characteristics of corrosion scale in drinking water distribution systems].

Scanning electron microscopy, X-ray fluorescence spectroscopy, X-ray diffraction and X-ray photoelectron spectroscopy were used to analyze the microstructure, chemical composition, crystalline structure and compound constitute of the corrosion scale from cast iron pipe and galvanized steel pipe in drinking water distribution systems. The outer of the corrosion scale was compact, while the inner was porous. Iron was the primary chemical element of the corrosion scale, and the composition of the scale was iron compounds. The outer scale were ferric compounds such as alpha-FeOOH, gamma-FeOOH, alpha-Fe2O3, gamma-Fe2O3, FeCl3, while the inner were ferrous compounds such as Fe3O4, FeCl2, FeCO3. The characteristics of the corrosion scale was lying on hydraulic conditions and water quality in distribution systems, and the characteristics of iron pipe materials.

Corrosion↗
PubMed1986

On the molecular mechanism of lactoperoxidase-catalyzed H2O2 metabolism and irreversible enzyme inactivation.

Lactoperoxidase-catalyzed H2O2 metabolism proceeds through one of three different pathways, depending on the nature and the concentration of the second substrate as an e- donor and/or on pH conditions. In the lactoperoxidase (LPO)-H2O2 system, at low H2O2 concentrations and/or alkaline conditions the peroxidatic cycle involves ferric LPO----compound I----compound II----ferric LPO conversion, whereas high H2O2 concentrations and/or acidic conditions favor the ferric LPO----compound I----compound II----compound III----ferrous LPO----ferric LPO pathway. The compound III/ferroperoxidase states are associated with irreversible enzyme inactivation by cleavage of the heme moiety and liberation of iron. It is likely that either singlet oxygen or superoxide and hydroxyl radicals are involved in the attack on heme iron, because inactivation correlates with oxygen production and can be decreased to a certain degree by scavengers such as ethanol, 1-propanol, 2-propanol, or mannitol. In the LPO-H2O2-I- system, the enzyme may also be inactivated by I2 generated in the course of enzymatic I- oxidation (i.e. during ferric LPO----compound I----ferric LPO cycles).

Ferric Compounds↗
PubMed1988

Synthesis, effectiveness and metabolic fate in cows of the caesium complexing compound ammonium ferric hexacyanoferrate labelled with 14C.

Adding ammonium ferric hexacyanoferrate (AFCF) to cows' fodder produced after the Chernobyl nuclear accident prevented milk contamination by increasing the faecal elimination of 137Cs. Synthesis of ammonium ferric hexa[14C]-cyanoferrate (AF14CF) and its purification were performed for the study of the metabolic fate of this complex, and the evaluation of the possible release of cyanide. The stability of this colloidal product, tested by anaerobic incubation in rumen juice in vitro, showed no release of free cyanide from AF14CF, but hexacyanoferrate was identified in the rumen juice and 0.13% of the added radioactivity was converted to labelled CO2. AF14CF administered per os to two cows showed a nearly quantitative excretion of radioactivity in faeces during the first 3 d (91-95%). A very low but significant level of radioactivity appeared in plasma, blood cells, expired CO2 and was detected in organs taken 9 d after administration. Total cumulative radioactivity in urine and milk amounted to 0.19-0.47% and 0.068-0.071% respectively for the two cows. Labelled hexacyanoferrate and thiocyanate were identified in the urine and also in faeces. In spite of this relative instability of AFCF in the rumen of cows, the poor absorption of AF14CF degradation products showed that AFCF constitutes an efficient and safe food additive to prevent the absorption of radioactive caesium from ruminant feed and its secretion in milk.

Accidents↗
PubMed2005

Interactions of ferric ions with olive oil phenolic compounds.

The ferric complexing capacity of four phenolic compounds, occurring in olives and virgin olive oil, namely, oleuropein, hydroxytyrosol, 3,4-dihydroxyphenylethanol-elenolic acid (3,4-DHPEA-EA), and 3,4-dihydroxyphenylethanol-elenolic acid dialdehyde (3,4-DHPEA-EDA), and their stability in the presence of ferric ions were studied. At pH 3.5, all compounds formed a reversible 1:1 complex with ferric ions, but hydroxytyrosol could also form complexes containing >1 ferric ion per phenol molecule. At pH 5.5, the complexes between ferric ions and 3,4-DHPEA-EA or 3,4-DHPEA-EDA were relatively stable, indicating that the antioxidant activity of 3,4-DHPEA-EA or 3,4-DHPEA-EDA at pH 5.5 is partly due to their metal-chelating activity. At pH 7.4, a complex containing >1 ferric ion per phenol molecule was formed with hydroxytyrosol. Oleuropein, 3,4-DHPEA-EA, and 3,4-DHPEA-EDA also formed insoluble complexes at this pH. There was no evidence for chelation of Fe(II) by hydroxytyrosol or its derivatives. At all pH values tested, hydroxytyrosol was the most stable compound in the absence of Fe(III) but the most sensitive to the presence of Fe(III).

Drug Stability↗
PubMed1990

[Study on adhesion mechanism of MMA-TBBO resin to dentin. A model experiment using decalcified dentin].

As a model experiment to understand the mechanism of adhesion of the MMA-TBBO resin to dentin, MMA-TBBO was polymerized using a decalcified dentin sheet treated with aqueous citric acid (CA) solutions of copper fluoride (CF), ferric fluoride (FF), or ferric chloride (FC), which are usually used as treating agents in the bonding of the resin to dentin. The curing time for MMA-TBBO resin was considerably reduced on the decalcified dentin sheet treated with FC-CA, CF-CA or FF-CA at an appropriate concentration. Polymerization of MMA-TBBO resin was accelerated in the presence of a fluoride ion. Molecular weight of PMMA depended on the site of polymerization; PMMA polymerization inside the decalcified dentin sheet gave the highest and that outside gave the lowest molecular weight in the presence of an appropriate amount of ferric or cupric ion. These results suggested that ferric compounds adsorbed to decalcified dentin are involved in the polymerization of MMA and thus will influence the bond strength of the MMA-TBBO resin to dentin.

Acrylic Resins↗
PubMed1991

Evidence for regulatory control of iron uptake from ferric maltol across the small intestine of the rat.

1. 59Fe absorption from the novel iron compound, ferric maltol, was studied in rats pretreated twice daily for two weeks with non-radioactive ferric maltol in oral doses containing 7 mg elemental iron. Tissue accumulation of 59Fe 2 h after administration of radioactive ferric maltol into the stomach was significantly lower in iron pretreated animals than in saline-treated controls. 2. 59Fe uptake from ferric maltol into isolated fragments of ileum and of duodenum was of similar magnitude in control animals but in iron-treated animals, duodenal uptake was significantly lower than that of the ileum. 3. Absorption of 59Fe was also investigated in anaesthetized rats after intestinal perfusion with saline (controls) or with 5 mM chenodeoxycholate to render the intestines more permeable. 4. Changes in permeability of the small intestine were monitored by estimating the amount of [14C]-mannitol absorbed and fluid secreted with reference to the non-absorbable [3H]-inulin in the perfusate effluents. 5. Despite the increased permeability of the intestines after bile salt treatment, there was little difference from control in the tissue accumulation of 59Fe from ferric maltol 2 h after intraduodenal administration. However 59Fe absorption from ferrous sulphate was significantly increased after bile salt treatment. 6. Gel filtration profiles of plasma made 5 and 60 min after intraduodenal administration of [59Fe]-ferric [3H]-maltol demonstrated that metal and ligand do not enter the circulation as the complex even when intestinal permeability is increased. 7. Uptake of 59Fe was investigated in isolated fragments of rat small intestine after saline or bile salt perfusion. Although 59Fe uptake from ferric maltol was somewhat greater in the bile salt-treated intestinal fragments, saturable kinetics were still observed. By contrast, "Fe uptake from ferrous sulphate: ascorbate was greatly enhanced by bile salt pretreatment and a very large diffusional component of uptake was evident. 8. It is concluded that iron uptake from ferric maltol may well be under endogenous regulatory control even in damaged intestines, so it is unlikely that this novel iron compound can bring about iron overload when administered orally.

Animals↗
PubMed2005

Spectroscopic studies of the anaerobic enzyme-substrate complex of catechol 1,2-dioxygenase.

The basis of the respective regiospecificities of intradiol and extradiol dioxygenase is poorly understood and may be linked to the protonation state of the bidentate-bound catechol in the enzyme/substrate complex. Previous ultraviolet resonance Raman (UVRR) and UV-visible (UV-vis) difference spectroscopic studies demonstrated that, in extradiol dioxygenases, the catechol is bound to the Fe(II) as a monoanion. In this study, we use the same approaches to demonstrate that, in catechol 1,2-dioxygenase (C12O), an intradiol enzyme, the catechol binds to the Fe(III) as a dianion. Specifically, features at 290 nm and 1550 cm(-1) in the UV-vis and UVRR difference spectra, respectively, are assigned to dianionic catechol based on spectra of the model compound, ferric tris(catecholate). The UVRR spectroscopic band assignments are corroborated by density functional theory (DFT) calculations. In addition, negative features at 240 nm in UV-vis difference spectra and at 1600, 1210, and 1175 cm(-1) in UVRR difference spectra match those of a tyrosinate model compound, consistent with protonation of the axial tyrosinate ligand when it is displaced from the ferric ion coordination sphere upon substrate binding. The DFT calculations ascribe the asymmetry of the bound dianionic substrate to the trans donor effect of an equatorially ligated tyrosinate ligand. In addition, the computations suggest that trans donation from the tyrosinate ligand may facilitate charge transfer from the substrate to yield the iron-bound semiquinone transition state, which is capable of reacting with dioxygen. In illustrating the importance of ligand trans effects in a biological system, the current study demonstrates the power of combining difference UVRR and optical spectroscopies to probe metal ligation in solution.

Anaerobiosis↗