Studies on metal carboxylates. VIII. Reactions of acetylacetonates of the first row transition elements with pyridine-2,6-dicarboxylic acid

The acetylacetonates VO(acac)₂, M(acac)₃, where M = V, Mn or Fe and [M′(acac)₂]_n, where M′ = Co, Ni or Cu, have been reacted with pyridine-2,6-dicarboxylic acid (dipicH₂) in acetone to afford the complexes VO(dipic)·2H₂O, M(acac)(dipic)·xH₂O [M = V, Mn or Fe and x = 1 or 0] and M₂(dipic) (dipicH)₂·yH₂O [M = Co, Ni or Cu and y = 2 or 0]. The cobalt(II) and nickel(II) complexes are converted to polymeric [M(dipic)]_n in ethanol and all three complexes formulated as M₂(dipic)(dipicH)₂ react with 2,2′2″-terpyridyl to yield M(dipic)(terpy)·3H₂O. The vanadium(III) complex V(acac)(dipic) is oxidized to VO(dipic)·4H₂O in aqueous solution via the vanadium(III) intermediate V(OH)(dipic)·2H₂O. Tentative structural conclusions are drawn for certain of these new complexes based upon room temperature spectral and magnetic measurements. The characterization of these complexes has included selected studies of their X-ray photoelectron spectra.     

The hemoglobin of the crossopterygian fish, Latimeria chalumnae (Smith). Subunit structure and oxygen equilibria

There are five oxidation-reduction states of horseradish peroxidase which are interconvertible. These states are ferrous, ferric, Compound II (ferryl), Compound I (primary compound of peroxidase and H₂O₂), and Compound III (oxy-ferrous). The presence of heme-linked ionization groups was confirmed in the ferrous enzyme by spectrophotometric and pH stat titration experiments. The values of pK were 5.87 for isoenzyme A and 7.17 for isoenzymes (B + C). The proton was released when the ferrous enzyme was oxidized to the ferric enzyme while the uptake of the proton occurred when the ferrous enzyme reacted with oxygen to form Compound III. The results could be explained by assuming that the heme-linked ionization group is in the vicinity of the sixth ligand and forms a stable hydrogen bond with the ligand.The measurements of uptake and release of protons in various reactions also yielded the following stoichiometries: Ferric peroxidase + H₂O₂ → Compound I, Compound I + e^? + H⁺ → Compound II, Compound II + e^? + H⁺ → ferric peroxidase, Compound II + H₂O₂ → Compound III, Compound III + 3e^? + 3H⁺ → ferric peroxidase.Based on the above stoichiometries and assuming the interaction between the sixth ligand and heme-linked ionization group of the protein, it was possible to picture simple models showing structural relations between five oxidation-reduction states of peroxidase. Tentative formulae are as follows: [Pr·Po·Fe-(II) $\text{\$}\text{?}$PrH⁺·Po·Fe(II)] is for the ferrous enzyme, Pr·Po·Fe(III)OH₂ for the ferric one, Pr·Po·Fe(IV)OH^? for Compound II, Pr(OH^?)·Po⁺·Fe(IV)OH^? for Compound I, and PrH⁺·Po·Fe(III)O₂^? for Compound III, in which Pr stands for protein and Po for porphyrin. And by Fe(IV)OH^?, for instance, is meant that OH^? is coordinated at the sixth position of the heme iron and the formal oxidation state of the iron is four.     

Infrared and raman spectra of metal 1,2,4,5-benzenetetracarboxylates: Evidence for very short,strong hydrogen bonds

Salts of 1,2,4,5-benzenetetracarboxylic acid with copper, aluminum, ammonium, cobalt(II), thallium(I), tin(II), uranyl ion, zinc, manganese, iron(II), nickel, potassium and sodium have been prepared and characterized by their IR spectra. The salts of aluminum, ammonium, thallium(I), tin(II), zinc, iron(II), nickel, potassium and sodium had not been reported before with adequate characterization. Raman spectra of selected compounds also aided structural interpretation. The IR spectra of Na₂C₁₀H₄O₈·2H₂O, Fe(C₁₀H₅O₈)₂·12H₂O, Zn(C₁₀H₅O₈)₂·12H₂O, Ni(C₁₀H₅O₈)₂·12H₂O, (NH₄)₃C₁₀H₃O₈·H₂O and CoC₁₀H₄O₈·6H₂O indicate very short, strong hydrogen bonds in these compounds. The IR and Raman spectra can be used to determine the mode of coordination (if any) of the carboxylate groups of 1,2,4,5- benzenetetracarboxylate to metal ions.     

Sugar complexes with alkaline earth metal ions. Synthesis,structure, and spectroscopic studies of Mg(II), Sr(II), and Ba(II) complexes of d-glucur

Interaction between D-glucuronic acid and alkaline earth metal ions leads to the formation of the complexes such as M(D-glucuronate)X· nH₂O and M(D-glucuronate)₂ · nH₂O, where M = Mg(II), Sr(II), and Ba(II), X = Cl^? or Br^?, and n = 2–4. Owing to the distinct spectral similarities with the structurally known Ca(D-gluguronate)Br · 3H₂O compound, the metal cations bind to three sugar moieties (through O₆, O₅ of the first, O₆', O₄ of the second, and O₁, O₂ of the third residue) and to two H₂O molecules, forming an eight-coordination geometry around each metal ion, in M(D-glucuronate)X · nH₂O (except for Mg(II) ion, which is six-coordination). The metal ions in M(D-glucuronate)₂-nH₂O show six-coordination in different structural environments. The strong hydrogen bonding network of the free acid is weakened upon metalation and the sugar moiety crystallizes as α-anomer, in these series of metal-sugar complexes.     

Chemical evolution of iron containing enzymes: Mixed ligand complexes of iron as intermediary steps

Activities of the iron complexes of evolutionary importance like K₄[Fe(CN)₆], K₄[Fe(CN)₅(gly)], and K₄[Fe(CN)₅(trigly)] have been tested towards some redox reactions of biological significance, namely, decomposition of hydrogen peroxide, dehydrogenation of NADH and ascorbic acid both coupled with reduction of methylene blue. It has been observed that the catalytic activities of iron (II) complexes towards the redox reactions studied at pH 9.18 followed the order, K₄[Fe(CN)₆]4[Fe(CN)₅(gly)]4[Fe(CN)₅(trigly)]. Decomposition of H₂O₂ catalysed by cyanocomplexes of iron (II) has been discussed through the formation of an innersphere complex in which loosly bound ligands like, glycine and triglycine are replaced by hydroperoxide ion. A tentative mechanism for the catalysed decomposition of H₂O₂ has been discussed.Based upon the experimental observations a hypothesis on the evolution of iron containing enzymes has been envisaged as: iron(II) ion iron(II) cyanide complexes mixed ligand iron(II) cyanide and amino acid complexes iron(II) complexes of macromolecules proenzyme or early enzyme containing iron(II).     

Reduction of methemerythrin by dithionite ion

The reduction of methemerythrin (Hr⁺) by dithionite produces deoxyhemerythrin (Hr^o) in multi, possibly three, stages. The kinetics were examined at pH 8·2 and 25 °C. The first stage is reduction of methemerythrin to an intermediate A by SO₂^- (k = 1.3 × 10⁵m^?1s^?1). The much slower second and third stages have rates independent of dithionite concentrations. Reaction is completed after about 10 h. The kinetics of reactions of A with N₃^-, H₂O₂, and O₂ were examined, as well as the conversion of A to intermediate B (k = 4·4 × 10^?4s^?1). It is concluded that A is an (Fe(II)Fe(III))₈ species, and that in B the unit (Fe(II)Fe(II))₈ is well developed, judging by its unreactivity towards N₃^?, its reaction with H₂O₂, and its reversible uptake of O₂ (85–90% of the final product). There is little effect of adjusting the pH to 6·3 on the rates of the processes examined.     

Sugar interaction with metal ions: synthesis,spectroscopic, and structural analysis of Zn(II), Cd(II), and Hg(II) complexes,containing d-glucuronate anion

Interaction between D-glucuronic acid and Zn(II), Cd(II), and Hg(II) metal ion salts has been studied in solution and solid complexes of the type M(D-glucuronate)X · nH₂O and M(D-glucuronate)₂·nH₂O, where M = Zn(II), Cd(II), and Hg(II), X = Cl⁻ or Br⁻, and n = 0–2 were isolated and characterized. Spectroscopic and other evidence indicated that in the metal-halide-sugar complexes the Zn(II) and Cd(II) ions bind to two D-glucuronate moieties via 06, 05 of the carboxyl oxygen atoms of the first and 04, 06' of hydroxyl and carbonyl groups of the second as well as to two H₂O molecules, whereas in the corresponding M(D-glucuronate)₂ · nH₂O salts, the metal ions are bonded to two sugar anions through 06 and 06' of the ionized carboxyl groups and two water molecules, resulting in a six-coordination around each metal cation. The Hg(II) ion binds to 06 and 05 oxygen atoms of a sugar anion and to a halide anion or water molecule, in the Hg(D-glucuronate)X·nH₂O compounds, while in the corresponding metal-glucuronate salt mercury is bonded to 06 and 06' of the two glucuronate anions with four-coordination around the Hg(II) ion. The β-anomer sugar conformation is predominant in the free acid and in these series of metal-sugar complexes.     

Synthesis,characterization and antitumor activity of some metal complexes of 3- and 5-substituted salicylaldehyde o-hydroxybenzoylhydrazones

Complexes of Mn(II), Fe(III), Fe(II), Co(II), Ni(II), Cu(II), Zn(II) and Pt(II) with 3- and 5-substituted salicylaldehyde o-hydroxybenzoylhydrazones (XSBH, X = H, 3-NO₂, 3-CH₃O, 5-Cl, 5-Br, 5-CH₃ or 5-NO₂) have been prepared and characterized by elemental analysis, conductance measurements, magnetic susceptibilities (from room temperature down to liquid nitrogen temperature) and spectral studies. These studies indicate the following structures: monomeric, high-spin, distorted octahedral for Mn(XSBH)₂; monomeric, high-spin, five-coordinate for Fe(XSBH)SO₄·H₂O; dimeric, high-spin phenoxide bridged, five-coordinate for Fe(XSBH)Cl; dimeric, high-spin five-coordinate for Co(XSBH)Cl·2H₂O; dimeric low-spin, five-coordinate for Ni(XSBH)Cl·2H₂O; dimeric, four-coordinate for Zn(XSBH); and a square-planar structure for M(XSBH)Cl·H₂O (M = Cu(II) or Pt(II).Intermolecular antiferromagnetic exchange interactions are present in Fe(III) complexes, where the exchange parameter (J) is ca. −8.0 cm⁻¹ for these complexes. The Fe(III) complexes exhibit asymmetric quadrupole split doublets in their ⁵⁷Fe Mössbauer spectra. The asymmetry is found to be temperature dependent with relatively symmetrical doublets seen at low temperature. The polycrystalline ESR spectra of Cu(II) complexes are isotropic and indicate a d_x²−y² ground state in square-planar stereo-chemistry. All these metal complexes have been screened for their antitumor activity against the P 388 lymphocytic leukaemia test system in mice and enhanced antitumor activity relative to the free ligand was found but no significant activity at the dosages used.     

Kinetic simulation studies on the transient formation of the oxo‐iron(IV) porphyrin radical cation during the reaction of iron(III) tetrakis‐5,10,15,20‐(N‐methyl‐4‐pyridyl)‐porphyrin with hydrogen peroxide in aqueous solution

High‐valent oxo‐iron(IV) species are commonly proposed as the key intermediates in the catalytic mechanisms of iron enzymes. Water‐soluble iron(III) tetrakis‐5,10,15,20‐(N‐methyl‐4‐pyridyl)porphyrin (Fe(III)TMPyP) has been used as a model of heme‐enzyme to catalyse the hydrogen peroxide (H₂O₂) oxidation of various organic compounds. However, the mechanism of the reaction of Fe(III)TMPyP with H₂O₂ has not been fully established. In this study, we have explored the kinetic simulation of the reaction of Fe(III)TMPyP with H₂O₂ and of the catalytic reactivity of FeTMPyP in the luminescent peroxidation of luminol. According to the mechanism that has been established in this work, Fe(III)TMPyP is oxidized by H₂O₂ to produce (TMPyP)^·+Fe(IV)=O (k1 = 4.5 × 10⁴/mol/L/s) as a precursor of TMPyPFe(IV)=O. The intermediate, (TMPyP)^·+Fe(IV)=O, represented nearly 2% of Fe(III)TMPyP but it does not accumulate in suf?cient concentration to be detected because its decay rate is too fast. Kinetic simulations showed that the proposed scheme is capable of reproducing the observed time courses of FeTMPyP in various oxidation states and the decay pro?les of the luminol chemiluminescence. It also shows that (TMPyP)^·+Fe(IV)=O is 100 times more reactive than TMPyPFe(IV)=O in most of the reactions. These two species are responsible for the initial sharp and the sustained luminol emissions, respectively. Copyright © 2003 John Wiley & Sons, Ltd.     

Localization of repetitive and unique DNA sequences neighbouring the rabbit beta-globin gene

The structure of oxymyoglobin has been refined at 1·6 Å resolution, using diffractometer data collected at ?12 °C. The crystallographic R factor is 0·159, and the atomic positions are known to 0·1 Å accuracy in internal segments of the molecule.The iron atom lies 0·22(3) Å from the plane of the porphyrin, 0·25 Å closer than in deoxymyoglobin, and the F helix has moved by a similar amount. Oxygen binds to the iron in a bent, end-on arrangement, with FeOO = 115(5) ° and FeO = 1·83(6) Å. The mean FeN(porphyrin) bond length is 1·95(6) Å, 0·08 Å shorter than in deoxymyoglobin, but the difference is not significant compared to the experimental error. FeN_ε(His8F) is 2·07(6) Å, the same as in model compounds. Movements of the haem, iron, F helix and FG corner on oxygenation are similar to those found in the T-R state transition in haemoglobin, but are smaller in magnitude.     

Synthesis and studies of some bivalent transition metal complexes with acylhydrazones

Complexes of 3-hydroxy-2-naphthaldehyde benzylhydrazone (H₂nabh) and 3-hydroxy-2-naphthaldehyde salicyloylhydrazone (H₃nash) of the empirical composition M(L2H)·nH₂O [M = manganese(II), iron(II), cobalt(II), nickel(II), copper(II), zinc(II), cadmium(II), mercury(II), L = H₂nabh, H₃nash and n = 0, 1, 2] were prepared and characterized by elemental analyses, magnetic susceptibility, electronic and infrared spectral data. Zinc(II) and cadmium(II) complexes were also studied by ¹³C, ¹H NMR and the Cu(nabh)·H₂O complex by transmission electron microscopy. The complexes are coloured and highly insoluble in common organic solvents. Absence of the original anion in the complexes indicates deprotonation of the ligands (H₂nabh and H₃nash) which bind the metal ions from the OH and the CN groups.     

Synthesis of metal paddlanes: X-ray structure determination of bis-(methyl nicotinate)copper(II) acetate dimer

The synthesis of nicotinic acid based N,N′-bidentate ligands capable of spanning the axial sites of copper(II) acetate dimer are reported. Reaction of these ligands with [Cu(C₂H₃0₂)₂]₂·2H₂0 gave the 1:1 adduct: a metal paddlane, which on recrystallization from MeOH/CHCl₃ yielded the trans-esterified complex [Cu(C₂H₃O₂)₂]₂·2C₇H₇N0₂, 3. A single crystal X-ray structure determination of 3 is presented.     

Transient formation of the oxo–iron(IV) porphyrin radical cation during the reaction of iron(III) tetrakis‐5,10,15,20‐(N‐methyl‐4‐pyridyl)porphyrin with hydrogen peroxide in aqueous solution

The reaction of iron(III) tetrakis‐5,10,15,20‐(N‐methyl‐4‐pyridyl)porphyrin (Fe(III)TMPyP) with hydrogen peroxide (H₂O₂) and the catalytic activity of the reaction intermediates on the luminescent peroxidation of luminol in aqueous solution were studied by using a double‐mixing stopped‐flow system. The observed luminescence intensities showed biphasic decay depending on the conditions. The initial flashlight decayed within <1 s followed by a sustained emission for more than 30 s. Computer deconvolution of the time‐resolved absorption spectra under the same conditions revealed that the initial flashlight appeared during the formation of the oxo–iron(IV) porphyrin, TMPyPFe(IV) = O, which is responsible for the sustained emission. The absorption spectra 0.0–0.5 s did not reproduce well by a simple combination of the two spectra of Fe(III)TMPyP and TMPyPFe(IV) = O, indicating that transient species was formed at the initial stage. Addition of uric acid (UA) caused a significant delay in the initiation of the luminol emission as well as in the formation of the TMPyPFe(IV) = O. Both of them were completely diminished in the presence of UA equimolar with H₂O₂, while mannitol had no effect at all. The delay of the light emission as well as the appearance of TMPyPFe(IV) = O was directly proportional to the [UA]₀ but other kinetic profiles were not changed significantly. Based on these observations and the kinetic analysis, we confirmed the involvement of the oxo–iron(IV) porphyrin radical cation, (TMPyP)^·+Fe(IV) = O, as an obligatory intermediate in the rate‐determining step of the overall reaction, Fe(III)TMPyP + H₂O₂ → TMPyPFe(IV) = O, with a rate constant of k = 4.3 × 10⁴/mol/L/s. The rate constants for the reaction between the (TMPyP)^·+Fe(IV) = O and luminol, and between the TMPyPFe(IV) = O and luminol were estimated to be 3.6 × 10⁶/mol/L/s and 1.31 × 10⁴/mol/L/s, respectively. Copyright © 2003 John Wiley & Sons, Ltd.     

Reaction between iron(III) and pyrazoic acid

In the reaction of [Fe(H₂O)₆]³⁺ with pyrazoic acid, reduction of iron(III) to iron(II) is observed. When an excess of iron is present, the reaction involves a transfer of four electrons per mole of acid. At room temperature the redox reaction, which is dependent on hydrogen ion, iron(III) and pyrazoic acid concentrations, is rather slow and is the rate-determining step. The kinetic study was carried out at 50.0 ± 0.1 °C. The redox reaction is followed by a fast reaction of the iron(II) with an excess of ligand, resulting in the production of well-known complexes, where the acid acts as a chelating ligand through the nitrogen and oxygen atoms.     

Effects of road salt deicers on sediment biogeochemistry

Road salt deicers, especially NaCl and CaCl₂, are increasingly applied to paved areas throughout the world. The goal of this study is to investigate the influence of high concentrations of these salts on wetland biogeochemistry. Sediment cores were collected in fall and spring from a freshwater wetland fringing an urban kettle lake (Asylum Lake, Kalamazoo, MI, USA), and incubated for 100 days in deionized water (control) or with treatments of 1 or 5 g/L CaCl₂·2H₂O or 5 g/L NaCl to simulate addition of road salt deciers. At monthly intervals, cores were sliced into three depths (0–5, 5–10, 10–15 cm) and pore waters extracted for analysis of pH, total alkalinity and dissolved Mn(II), Fe(II), PO ₄ ^?3 , NH₃, H₂S, SO₄ ^?2, Na, K, Mg, and Ca. Changes in solid phase geochemistry were assessed by measuring the percent organic matter and the distribution of Fe and Mn among four operationally defined sediment fractions (exchangeable, carbonate, reducible, oxidizable) in the control and treatment cores. Addition of NaCl, and especially CaCl₂, stimulated significant growth of microbial mats at the core sediment–water interface and led to decreased pH and increased concentrations of Mn(II), Fe(II) and exchangeable cations (Ca, Mg, K, Na) in the sediment pore waters. This study demonstrates that the influx of road salt deciers is likely to have a significant impact on biogeochemical cycling in wetland sediments.     

Partitioning of taxifolin-iron ions complexes in octanol-water system

The composition of taxifolin-iron ions complexes in an octanol-water biphasic system was studied using the method of absorption spectrophotometry. It was found that at pH 5.0 in an aqueous biphasic system the complex of [Tf · Fe₂(OH) _k (H₂O)_{8 ? k} ] is present, but at pH 7.0 and 9.0 the complexes of [Tf₂ · Fe(OH) _k (H₂O)_{2 ? k} ] and [Tf · Fe(OH) _k (H₂O)_{4 ? k} ] are predominantly observed. The formation of a stable [Tf₃ · Fe] complex occurred in octanol phase. The charged iron ion of this complex is surrounded by taxifolin molecules, which shield the iron ion from lipophilic solvent. During transition from water to octanol phase the changes of the composition of complexes are accompanied by reciprocal changes in portion of taxifolin and iron ions in these phases. It was shown that the portion of taxifolin in aqueous solution in the presence of iron ions is increased at high pH values, and the portion of iron ions is minimal at pH 7.0. In addition, the parameters of solubility limits of taxifoliniron ions complexes in an aqueous solution were determined. The data obtained gain a better understanding of the role of complexation of polyphenol with metal of variable valency in passive transport of flavonoids and metal ions across lipid membranes.     

Abatement of Sorbed Crude Oil by Heterogeneous Fenton Process Using A Contaminated Soil Pre-Impregnated with Dissolved Fe(II) and Humic Acid

Dissolved Fe(II) and humic acid (HA) were pre-impregnated into contaminated soil to catalyze hydrogen peroxide to remove crude oil (CO). The effects of parameters such as initial Fe(II), HA and H₂O₂ concentrations on the oxidation of total petroleum hydrocarbon (TPH) were investigated using response surface methodology based on Box–Behnken design. The rate of hydrogen peroxide decomposition is decreased by pre-impregnating with dissolved Fe(II) + HA compared with only pre-impregnated Fe(II) and modified Fenton (MF). Oxygen evolution is the predominant route of hydrogen peroxide decomposition at natural pH. Unlike O₂ evolution, the kinetics of hydroxyl radical (OH^?) production are clearly uncoupled from H₂O₂ decay in these systems. The steady-state hydroxyl radical production rate is higher in the systems with pre-impregnated dissolved Fe(II) and HA, and more significance is the decrease in detectable TPH (70.84% removal efficiency) when soil is pre-impregnated with dissolved 25 mM Fe(II) + 0.7 mg/mL HA, and with the application of 700 mM H₂O₂, possibly due to hydrogen peroxide catalyzed by the iron of this complex (CO-HA–Fe(II)) producing hydroxyl radical in close proximity to the CO. Meanwhile, the removal efficiency of C₂₁–C₃₀ is up to 65.69%, which is 2.6 times higher than that of the MF (25.52%).     

Fe(III) oxides protect fermenter–methanogen syntrophy against interruption by elemental sulfur via stiffening of Fe(II) sulfides produced by sulfur respiration

Thermosipho globiformans (rod-shaped thermophilic fermenter) and Methanocaldococcus jannaschii (coccal hyperthermophilic hydrogenotrophic methanogen) established H₂-mediated syntrophy at 68 °C, forming exopolysaccharide-based aggregates. Electron microscopy showed that the syntrophic partners connected to each other directly or via intercellular bridges made from flagella, which facilitated transfer of H₂. Elemental sulfur (S⁰) interrupted syntrophy; polysulfides abiotically formed from S⁰ intercepted electrons that were otherwise transferred to H⁺ to produce H₂, resulting in the generation of sulfide (sulfur respiration). However, Fe(III) oxides significantly reduced the interruption by S⁰, accompanied by stiffening of Fe(II) sulfides produced by the reduction of Fe(III) oxides with the sulfur respiration-generated sulfide. Sea sand replacing Fe(III) oxides failed to generate stiffening or protect the syntrophy. Several experimental results indicated that the stiffening of Fe(II) sulfides shielded the liquid from S⁰, resulting in methane production in the liquid. Field-emission scanning electron microscopy showed that the stiffened Fe(II) sulfides formed a network of spiny structures in which the microorganisms were buried. The individual fermenter rods likely produced Fe(II) sulfides on their surface and became local centers of a core of spiny structures, and the connection of these cores formed the network, which was macroscopically recognized as stiffening.     

Metal complexes with 2-(α-hydroxy-benzyl) thiamin pyrophosphate (HBTPP). Models for metal binding of thiamin enzymes

The reactions of MCl₂ (M = Zn²⁺, Cd²⁺, Hg²⁺) with 2-(α-hydroxy-benzyl)thiamin pyrophosphate (HBTPP) at various pH values (different protonation states) were studied in methanolic solutions. Solid complexes of formulae K[Zn(HBTPP) ⁻Cl₂ · H₂O_n, K₂[Cd(HBTPP)²⁻Cl₂ · 3H₂O_n, K₂[Hg(HBTPP)₂⁻Cl₂ · 3H₂O and Zn(HBTPP)₂⁰Cl₂ were isolated and characterized by elemental analysis and various NMR techniques, namely ¹³C NMR, ³¹P NMR, ¹¹³Cd NMR, ¹⁹⁹Hg NMR and ¹H NMR ROESY spectra in D₂O. The data provide evidence that Zn(II) in K[Zn(HBTPP) ⁻Cl2 · H₂O_n, and Cd(II) in K₂[Cd(HBTPP)²⁻Cl₂ · 3H₂O_n, are coordinated both to the pyrimidine N(1′) and to the pyrophosphate group. In contrast, Hg(II) in K₂[Hg(HBTPP)₂⁻Cl₂ · 3H₂O and Zn(II) in Zn(HBTPP)₂⁰Cl₂ are bound only to the N(1′) atom or to the pyrophosphate group, respectively.     

A chelate complex‐enhanced luminol system for selective determination of Co(II), Fe(II) and Cr(III)

A determination method for Co(II), Fe(II) and Cr(III) ions by luminol‐H₂O₂ system using chelating reagents is presented. A metal ion‐chelating ligand complex with a Co(II) ion and a chelating reagent like ethylenediaminetetraacetic acid (EDTA) produced highly enhanced chemiluminescence (CL) intensity as well as longer lifetime in the luminol‐H₂O₂ system compared to metals that exist as free ions. Whereas free Cu(II) and Pb(II) ions had a strong catalytic effect on the luminol‐H₂O₂ system, significantly, the complexes of Cu(II) and Pb(II) with chelating reagents lost their catalytic activity due to the chelating reagents acting as masking agents. Based on the observed phenomenon, it was possible to determine Co(II), Fe(II) and Cr(III) ions with enhanced sensitivity and selectivity using the chelating reagents of the luminol‐H₂O₂ system. The effects of ligand, H₂O₂ concentration, pH, buffer solution and concentrations of chelating reagents on CL intensity of the luminol‐H₂O₂ system were investigated and optimized for the determination of Co(II), Fe(II) and Cr(III) ions. Under optimized conditions, the calibration curve of metal ions was linear over the range of 2.0 × 10^‐8 to 2.0 × 10^‐5 M for Co(II), 1.0 × 10^‐7 to 2.0 × 10^‐5 M for Fe (II) and 2.0 × 10^‐7 to 1.0 × 10^‐4 M for Cr(III). Limits of detection (3σ/s) were 1.2 × 10^‐8, 4.0 × 10^‐8 and 1.2 × 10^‐7 M for Co(II), Fe(II) and Cr(III), respectively. Copyright © 2012 John Wiley & Sons, Ltd.