Adenosine adducts with first row transition metal perchlorates

Adducts of adenosine (ado) with 3d metal perchlorates were synthesized by refluxing mixtures of ligand and salt in ethanol-triethyl orthoformate. Metal(III) perchlorates formed adducts involving 2:3 metal to ado molar ratio (MCr, Fe), i.e., M2(ado)₃(ClO₄)₆·4H₂O, whereas 1:1 adducts were produced by metal(II) perchlorates, as follows: M(ado)(ClO₄)₂·2H₂0 (MMn, Co, Ni, Cu); and M(ado)(Cl0₄)₂ (MFe, Zn). All the new complexes seem to be polymeric, involving a linear chainlike backbone with single ado bridges between adjacent metal ions in most cases, i.e., −(-M-ado-)-_n. The coordination sphere of each metal ion is completed by terminal aqua, ado and, with the exception of the Cu²⁺ complex, −OClO₃ ligands, in the case of the hydrated new complexes. Ado would be binding through the N(1) and N(7) ring nitrogens, when functioning as bridging, bidentate. As regards the two water-free M(II) complexes (MFe, Zn), which are apparently distorted tetrahedral, the evidence available is interpreted in terms of the presence of tridentate bridging ado, binding through N(1), N(7) in the same fashion as above, and through one of the ribose hydroxyl oxygens, which form weaker bonds to M²⁺ ions located in a neighboring linear polymeric −(-M-ado-)-n unit; the coordination sphere in these complexes is completed by one −OClO₃ ligand.     

Metal–bipyridine complexes in DNA backbones and effects on thermal stability

Modified oligonucleotides are showing potential for multiple applications, including drug design, nanoscale building blocks, and biosensors. In an effort to expand the functionality available to DNA, we have placed chelating ligands directly into the backbone of DNA. Between one and three nucleosides were replaced with 2,2′-bipyridine phosphates in 23-mer duplexes of DNA. An array of metal ions were added (Fe²⁺, Co²⁺, Ni²⁺, Cu²⁺, Zn²⁺, and Pt²⁺) and the influences on duplex stability were examined by melting temperature studies. Titrations and UV–vis absorption spectroscopy were used to provide insights into the nature of the metal complexes formed. We found that Ni²⁺ binding to 2,2′-bipyridine typically provided the greatest increase in duplex stability relative to the other metal ions examined. For example, addition of Ni²⁺ to one 2,2′-bipyridine–DNA duplex increased the melting temperature by 13 °C, from 65.0 ± 0.3 to 78.4 ± 0.9 °C. These studies show that metal ions and backbone ligands can be used to regulate DNA structure and stability.     

The Isolation of Collagenase and Its Enzymological and Physico-chemical Properties

A collagenolytic enzyme specific for native collagen and gelatin was isolated from Pseudomonas marinoglutinosa by DEAE-cellulose column chromatography, Sephadex G–150 gel filtration and by disc electrophoresis on polyacrylamide gel.

The molecular weight of the enzyme was approximately 74,000 and its isoelectric point was found to be around 4.5. The optimum pH and temperature for Z–GPLGP hydrolysis were around 7.6 and 38°C, respectively. The enzyme was rather stable up to 50°C and in the range between pH 5.0 and 10.0, and was stabilized by Ca²⁺ to some extent. Some chelating agents and metal ions such as Hg²⁺, Pb²⁺, Zn²⁺, Ni²⁺ and Fe²⁺ inactivated the enzyme, but diisopropyl phosphofluoridate, sulfhydryl agents and some trypsin inhibitors did not affect the activity.

The EDTA-inactivated enzyme was restored its activity by added Ca-salt to almost completely and very slightly by Co-, Mn- and Sr-salt.

Metal analysis showed the enzyme contained 1 g atom of zinc and 4 g atoms of calcium per mole.     

Correlation of proton release and ultraviolet difference spectra associated with metal binding by transferrin

A variety of metal ions can bind to the iron-transport protein, transferrin, at two specific sites. For each metal ion, a carboxylate anion is concomitantly bound. Six metal ions which were examined fall into two classes based on proton release and ultraviolet spectral changes which accompany binding to the protein. Class II ions, which include Cu²⁺ and Zn²⁺, release approximately 2 H⁺/metal bond. Class III ions, which include Fe³⁺, Ga³⁺, Al³⁺, and VO²⁺, release approximately 3 H⁺/metal bound. The increase in absorbance near 242 nm, characteristic of tyrosine ionization, has the ratio 0.55–0.75 for class II:class III ions. Both Fe³⁺ and Cu²⁺ form metal-transferrin-oxalate complexes in the presence of excess C₂O₄^2?. Fe³⁺ releases close to 3 H⁺/metal whether forming oxalate or bicarbonate complexes with transferrin. Binding of Cu²⁺ to transferrin releases 2 H⁺/metal in the presence of C₂O^2?₄ or HCO₃^?. Since equal numbers of H⁺/metal are released for both anions, it is likely that the bicarbonate ion does not lose its proton, and remains as HCO₃^? in transferrin. These results are interpreted in terms of possible combinations of ligands at the metal binding sites.     

Metal complexes of polyesters

Polyesters obtained from 2,5-dihydroxyterephthalic acid and 1,n-alkanediols were used to complexate the metal ions Mg²⁺, Ca²⁺, Sn²⁺, Pb²⁺, Ga³⁺, In³⁺, Bi³⁺, Si⁴⁺, Ce³⁺, UO₂²⁺, Mn²⁺, Mn³⁺, Co²⁺, Ni²⁺, Cu²⁺, Zn²⁺ and Cd²⁺. The metal ions are always six-coordinated with additional ligands (mostly H₂O) besides the four from the polyester system. The H₂O-ligands can be removed by heating in vacuum, as was proven for the complexes of Mn²⁺, Co²⁺, Ni²⁺ and Cu²⁺, and are added again in moist air. For the waterfree Ni²⁺-complex a tetrahedral surrounding is suggested by magnetic measurements. Polymerization degrees of the polyesters were found to be 30–70 by the membrane osmometric method. Thermal stabilities of the metal complexes (200– 300 °C) are less than those of the polyesters themselves (300–350 °C).     

Purification and biochemical characterization of a broad substrate specificity thermostable alkaline protease from Aspergillus nidulans

Aspergillus nidulans PW1 produces an extracellular carboxylesterase activity that acts on several lipid esters when cultured in liquid media containing olive oil as a carbon source. The enzyme was purified by gel filtration and ion exchange chromatography. It has an apparent MW and pI of 37 kDa and 4.5, respectively. The enzyme efficiently hydrolyzed all assayed glycerides, but showed preference toward short- and medium-length chain fatty acid esters. Maximum activity was obtained at pH 8.5 at 40°C. The enzyme retained activity after incubation at pHs ranging from 8 to11 for 12 h at 37°C and 6 to 8 for 24 h at 37°C. It retained 80% of its activity after incubation at 30 to 70°C for 30 min and lost 50% of its activity after incubation for 15 min at 80°C. Noticeable activation of the enzyme is observed when Fe²⁺ ion is present at a concentration of 1 mM. Inhibition of the enzyme is observed in the presence of Cu²⁺, Fe³⁺, Hg²⁺, and Zn²⁺ ions. Even though the enzyme showed strong carboxylesterase activity, the deduced N-terminal amino acid sequence of the purified protein corresponded to the protease encoded by prtA gene.     

The interaction of transition metal ions with adenosine 5'-monophosphate

Several complexes of Mn²⁺, Fe²⁺, Zn²⁺, Pd²⁺, Cd²⁺, Pb²⁺, Ce²⁺, Pr³⁺, Sm³⁺, Tb³⁺, and Uo₂₂₊ metal ions with adenosine 5'-monophosphate have been isolated. The stoichiometry of all the complexes prepared were 1:1 metal to mononucleotide, respectively, and they were characterized by elemental analysis, infrared, electronic and fluorescence spectroscopy, conductivity, and magnetic measurements. Similarities among the spectra of the substances with structurally known metal-mononucleotide complexes suggest that the metal ions interact directly or indirectly with the N₇ of the purine ring and the phosphate group of the mononucleotide.     

Influence of metal ions on bioremediation activity of protocatechuate 3,4-dioxygenase from Stenotrophomonas maltophilia KB2

The aim of this paper was to describe the effect of various metal ions on the activity of protocatechuate 3,4-dioxygenase from Stenotrophomonas maltophilia KB2. We also compared activity of different dioxygenases isolated from this strain, in the presence of metal ions, after induction by various aromatic compounds. S. maltophilia KB2 degraded 13 mM 3,4-dihydroxybenzoate, 10 mM benzoic acid and 12 mM phenol within 24 h of incubation. In the presence of dihydroxybenzoate and benzoate, the activity of protocatechuate 3,4-dioxygenase and catechol 1,2-dioxygenase was observed. Although Fe³⁺, Cu²⁺, Zn²⁺, Co²⁺, Al³⁺, Cd²⁺, Ni²⁺ and Mn²⁺ ions caused 20–80 % inhibition of protocatechuate 3,4-dioxygenase activity, the above-mentioned metal ions (with the exception of Ni²⁺) inhibited catechol 1,2-dioxygenase to a lesser extent or even activate the enzyme. Retaining activity of at least one of three dioxygenases from strain KB2 in the presence of metal ions makes it an ideal bacterium for bioremediation of contaminated areas.     

New extracellular thermostable oxalate oxidase produced from endophytic Ochrobactrum intermedium CL6: Purification and biochemical characterization

Oxalate oxidase (EC 1.2.3.4) catalyzes the oxidative cleavage of oxalate to carbon dioxide with the reduction of molecular oxygen to hydrogen peroxide. Oxalate oxidase found its application in clinical assay for oxalate in blood and urine. This study describes the purification and biochemical characterization of an oxalate oxidase produced from an endophytic bacterium, Ochrobactrum intermedium CL6. The cell-free fermentation broth was subjected to two-step enzyme purification, which resulted in a 58.74-fold purification with 83% recovery. Specific activity of the final purified enzyme was 26.78 U?mg^?1 protein. The enzyme displayed an optimum pH and temperature of 3.8 and 80°C, respectively, and high stability at 4–80°C for 6?h. The enzymatic activity was not influenced by metal ions and chemical agents (K⁺, Na⁺, Zn²⁺, Fe³⁺, Mn²⁺, Mg²⁺, glucose, urea, lactate) commonly found in serum and urine, with Cu²⁺ being the exception. The enzyme appears to be a metalloprotein stimulated by Ca²⁺ and Fe²⁺. Its K_m and K_cat for oxalate were found to be 0.45?mM and 85?s^?1, respectively. This enzyme is the only known oxalate oxidase which did not show substrate inhibition up to a substrate concentration of 50?mM. Thermostability, kinetic properties, and the absence of substrate inhibition make this enzyme an ideal candidate for clinical applications.     

Fermentative production of extracellular amylase from novel amylase producer,Tuber maculatum mycelium,and its characterization

Abstract

Truffles are symbiotic hypogeous edible fungi (form of mushroom) that form filamentous mycelia in their initial phase of the growth cycle as well as a symbiotic association with host plant roots. In the present study, Tuber maculatum mycelia were isolated and tested for extracellular amylase production at different pH on solid agar medium. Furthermore, the mycelium was subjected to submerged fermentation for amylase production under different culture conditions such as variable carbon sources and their concentrations, initial medium pH, and incubation time. The optimized conditions after the experiments included soluble starch (0.5% w/v), initial medium pH of 7.0, and incubation time of 7 days, at room temperature (22?±?2?°C) under static conditions which resulted in 1.41?U/mL of amylase. The amylase thus obtained was further characterized for its biocatalytic properties and found to have an optimum activity at pH 5.0 and a temperature of 50?°C. The enzyme showed good thermostability at 50?°C by retaining 98% of the maximal activity after 100?min of incubation. The amylase activity was marginally enhanced in presence of Cu²⁺ and Na⁺ and slightly reduced by K⁺, Ca²⁺, Fe²⁺, Mg²⁺, Co²⁺, Zn²⁺, and Mn²⁺ ions at 1?mM concentration.     

A Review of: “HPLC of Biological Macromolecules (Methods and Applications) K.M. Goodring F.E. Regnier,Eds Marcel Dekker,New York, 1990; hardbound, 676 pages, $150”

An ionically unbound and thermostable polyphenol oxidase (PPO) was extracted from the leaf of Musa paradisiaca. The enzyme was purified 2.54-fold with a total yield of 9.5% by ammonium sulfate precipitation followed by Sephadex G-100 gel filtration chromatography. The purified enzyme exhibited a clear single band on native polyacrylamide gel electrophoresis (PAGE) and sodium dodecyl sulfate (SDS) PAGE. It was found to be monomeric protein with molecular mass of about 40 kD. The zymographic study using crude extract as enzyme source showed a very clear band around 40 kD and a faint band at around 15 kD, which might be isozymes. The enzyme was optimally active at pH 7.0 and 50°C temperature. The enzyme was active in wide range of pH (4.0–9.0) and temperature (30–90°C). From the thermal inactivation studies in the range 60–75°C, the half-life (t_1/2) values of the enzyme ranged from 17 to 77 min. The inactivation energy (Ea) value of PPO was estimated to be 91.3 kJ mol^?1. It showed higher specificity with catechol (K_m = 8 mM) as compared to 4-methylcatechol (K_m = 10 mM). Among metal ions and reagents tested, Cu²⁺, Fe²⁺, Hg²⁺, Mn²⁺, Ni²⁺, protocatechuic acid, and ferrulic acid enhanced the enzyme activity, while K⁺, Na⁺, Co²⁺, kojic acid, ascorbic acid, ethylenediamine tetraacetic acid (EDTA), sodium azide, β-mercaptoethanol, and L-cysteine inhibited the activity of the enzyme.     

Multifarious potential applications of keratinase of Bacillus subtilis K-5

Abstract

Bacillus subtilis K-5, an isolate from compost, utilized a wide range of keratinous wastes viz. diverse feather types, nails, hair, scales, etc. for growth and produced a thermostable alkaline protease (keratinase) with broad proteolytic activity. Optimization of cultural and environmental variables using a Plackett–Burman design and response surface methodology resulted in enhanced keratinase production (89%). Keratinase was partially purified (15-fold) by ammonium sulfate precipitation and carboxymethyl cellulose chromatography. The optimum pH and temperature for keratinase activity were 9.0 and 60°C, however, considerable activity and stability was observed over broad pH (5–10) and temperature range (50–90°C). B. subtilis K-5 keratinase exhibited excellent stability toward detergents (cetyl trimethylammonium bromide, Tween 80, and sodium dodecyl sulfate) and organic solvents (benzene, acetonitrile, phenylmethylsulfonyl fluoride); however, metal ions like Mn²⁺, Cu²⁺, Na⁺, Hg²⁺, K⁺, Ca²⁺, and Zn²⁺ inhibited the activity. B. subtilis K-5 protease showed remarkable potential for diverse applications like blood stain removal, gelatin hydrolysis from waste X-ray films and dehairing of animal hide.     

Biosorption of Heavy Metals (Cd2+, Cu2+, Co2+, and Mn2+) by Thermophilic Bacteria,Geobacillus thermantarcticus and Anoxybacillus amylolyticus: Equilibrium and Kinetic Studies

ABSTRACT

Two strains of thermophilic bacteria, Geobacillus thermantarcticus and Anoxybacillus amylolyticus, were employed to investigate the biosorption of heavy metals including Cd²⁺, Cu²⁺, Co²⁺, and Mn²⁺ ions. The effects of different biosorption parameters such as pH (2.0–10.0), initial metal concentrations (10.0–300.0 mg L^?1), amount of biomass (0.25–10 g L^?1), temperature (30–80°C), and contact time (15–120 min) were investigated. Concentrations of metal ions were determined by using an inductively coupled plasma optical emission spectrometry (ICP-OES). Optimum pHs for Cd²⁺, Cu²⁺, Co²⁺, and Mn²⁺ biosorption by Geobacillus thermantarcticus were found to be 4.0, 4.0, 5.0, and 6.0, respectively. For Anoxybacillus amylolyticus, the optimum pHs for Cd²⁺, Cu²⁺, Co²⁺, and Mn²⁺ biosorption were found to be 5.0, 4.0, 5.0, and 6.0, respectively. The Cd²⁺, Cu²⁺, Co²⁺, and Mn²⁺ removals at 50 mg L^?1 in 60 min by 50 mg dried cells of Geobacillus thermantarcticus were 85.4%, 46.3%, 43.6%, and 65.1%, respectively, whereas 74.1%, 39.8%, 35.1%, and 36.6%, respectively, for Anoxybacillus amylolyticus. The optimum temperatures for heavy metal biosorption were near the optimum growth temperatures for both strains. Scatchard plot analysis was employed to obtain more compact information about the interaction between metal ions and biosorbents. The plot results were further studied to determine if they fit Langmuir and Freundlich models.     

Purification and characterization of a novel phytase from Nocardia sp. MB 36

Phytase from Nocardia sp. MB 36 was purified (9.65-fold) to homogeneity by acetone precipitation, ion exchange, and molecular sieve chromatography. Native polyacrylamide gel electrophoresis (PAGE) and zymogram analysis showed a single active protein in the purified enzyme preparation. Sodium dodecyl sulfate (SDS)-PAGE analysis showed that phytase was a monomeric protein with a molecular weight of approximately 43 kDa. Phytase exhibited activity and stability over a broad pH range (2–8) and elevated temperatures (50–80°C), and utilized several phosphate compounds as substrates. Phytase was extremely resistant to pepsin and trypsin. Various metal ions viz. Fe²⁺, Co²⁺, and Mn²⁺, and NH₄⁺, ethylenediaminetetraacetic acid or EDTA and phenylmethylsulfonyl fluoride or PMSF had no influence on activity, while Ca²⁺ and Zn²⁺ enhanced activity by 15 % and 3.58 %, respectively. SDS caused significant reduction in enzyme activity (41.8 %), while 2,3-butanedione did so moderately (15.9 %). Features of Nocardia sp. MB 36 phytase suggest a potential for animal feed applications.     

Purification and Characterization of Microbial Protease Produced Extracellularly from <Emphasis Type="Italic">Bacillus subtilis</Emphasis> FBL-1

An ammonium sulfate precipitation of fermentation broth produced by Bacillus subtilis FBL-1 resulted in 2.9-fold increase of specific protease activity. An eluted protein fraction from the column chromatographies using DEAE-Cellulose and Sephadex G-75 had 94.2- and 94.9-fold higher specific protease activity, respectively. An SDS-PAGE revealed a band of purified protease at approximately 37.6 kDa. Although purified protease showed the highest activity at 45°C and pH 9.0, the activity remained stable in temperature range from 30 to 50°C and pH range from 7.0 to 9.0. Protease activity was activated by metal ions such as Ca²⁺, Mg²⁺, Mn²⁺, Fe²⁺, Ca²⁺ and K⁺, but 10 mM Fe³⁺ significantly inhibited enzyme activity (53%). Protease activity was inhibited by 2 mM EDTA as a metalloprotease inhibitor, but it showed good stability against surfactants and organic solvents. The preferred substrates for protease activity were found to be casein (100%) and soybean flour (71.6%).     

A Thermostable phytase from <Emphasis Type="Italic">Neosartorya spinosa</Emphasis> BCC 41923 and its expression in <Emphasis Type="Italic">Pichia pastoris</Emphasis>

A phytase gene was cloned from Neosartorya spinosa BCC 41923. The gene was 1,455 bp in size, and the mature protein contained a polypeptide of 439 amino acids. The deduced amino acid sequence contains the consensus motif (RHGXRXP) which is conserved among phytases and acid phosphatases. Five possible disulfide bonds and seven potential N-glycosylation sites have been predicted. The gene was expressed in Pichia pastoris KM71 as an extracellular enzyme. The purified enzyme had specific activity of 30.95 U/mg at 37°C and 38.62 U/mg at 42°C. Molecular weight of the deglycosylated recombinant phytase, determined by SDS-PAGE, was approximately 52 kDa. The optimum pH and temperature for activity were pH 5.5 and 50°C. The residual phytase activity remained over 80% of initial activity after the enzyme was stored in pH 3.0 to 7.0 for 1 h, and at 60% of initial activity after heating at 90°C for 20 min. The enzyme exhibited broad substrate specificity, with phytic acid as the most preferred substrate. Its K _m and V _max for sodium phytate were 1.39 mM and 434.78 U/mg, respectively. The enzyme was highly resistant to most metal ions tested, including Fe²⁺, Fe³⁺, and Al³⁺. When incubated with pepsin at a pepsin/phytase ratio of 0.02 (U/U) at 37°C for 2 h, 92% of its initial activity was retained. However, the enzyme was very sensitive to trypsin, as 5% of its initial activity was recovered after treating with trypsin at a trypsin/phytase ratio of 0.01 (U/U).     

Xanthine complexes with 3d metal perchlorates

Complexes of xanthine (xnH) with 3d metal perchlorates were prepared by refluxing mixtures of ligand and metal salt in ethyl acetate-triethyl orthoformate. In all cases, partial substitution of anionic xn⁻ for ClO₄⁻ groups occurs, and the solid complexes isolated also contain invariably two neutral xnH ligands per metal ion, viz. Cr(xn)₂(xnH)₂ClO₄, Fe(xn)₂(xnH)₂ClO₄·H₂O, M(xn)(xnH)₂ClO₄·H₂O (M = Fe, Co, Ni) and M(xn)(xnH)₂ClO₄· 2H₂O (M = Mn, Zn). The new complexes are generally hexacoordinated and appear to be linear chainlike polymeric species characterized by a (-Mxn-)_n single-bridged backbone. Four terminal ligands per metal ion, including two xnH groups in all cases, complete its inner coordination sphere; the remaining two terminal ligands differ from complex to complex as follows: M = Cr³⁺ xn⁻, -OClO₃; Fe³⁺ xn⁻, H₂O; Fe²⁺, Co²⁺, Ni²⁺OClO₃, H₂O; Mn²⁺, Zn²⁺ two aqua ligands. Probable binding sites of bidentate bridging xn⁻ and unidentate terminal xnH and xn⁻ are discussed.     

Selective binding of Ni2+ and Cu2+ metal ions with naphthazarin esters isolated from Arnebia euchroma

Naphthazarin esters (C1–C4) isolated from the roots of Arnebia euchroma are found as skilled dual chemosensors for Ni²⁺ and Cu²⁺ among Pb²⁺, Na²⁺, K²⁺, Hg²⁺, Mg²⁺, and Ca²⁺ metal ions. C1–C4 esters exhibited a red shift of 54 nm with Ni²⁺ and 30 nm with Cu²⁺ metal ions in absorption. There is a formation of red-shifted bands between 517 and 613 nm in the absorption spectrum of C1–C4 sensors on binding with Ni²⁺ and Cu²⁺ ions. The addition of Ni²⁺ and Cu²⁺ ions to sensors C1–C4 stimulates a remarkable color change from reddish pink to purple and light blue, respectively. These color changes can be identified with the naked eye. The significant downfield shifts of CO and OH peaks in nuclear magnetic resonance (NMR) spectrum confirm the chelation as binding mechanism. With ultraviolet–visble and NMR studies, it is found that C1–C4 esters possessed notable selectivity and sensitivity toward Ni²⁺ and Cu²⁺ over other metal ions.     

Continuous metal bioremoval by new bacterial isolates in immobilized cell reactor

In this study, four bacterial species isolated from an industrially polluted region at the Istanbul–Kocaeli border were characterized and their efficiencies for bioremoval of Cu²⁺, Ni²⁺, Cr³⁺, Zn²⁺, and Fe²⁺ were determined in batch and continuous systems. Strain N4c was used for continuous metal bioremoval in a packed-bed immobilized cell reactor (ICR) with a working volume of 180 ml. ICR was successfully operated for treatment of synthetic wastewater containing 200 mg/l Cu²⁺ and Ni²⁺ for 140 and 80 h, respectively. Bioremoval efficiency of ICR for Cu²⁺ reached around 90 % in the last 3 days of operation at a flow rate of 1 ml/min. Ni²⁺ bioremoval in ICR was less efficient as the system worked for only 80 h and bioremoval efficiency decreased from 73.3 to 42.8 % during the operation period. Wastewater containing one or two types of metal seems to be a good candidate for treatment with immobilized N4c cells in a continuous system. Survival of the cells in the wastewater was found to be an important parameter affecting bioremoval efficiency in both batch and continuous systems. The ICR used in this study can be scaled up for treatment of industrial wastewaters containing Ni²⁺ or Cu²⁺.     

Three colorimetric and off–on fluorescent chemosensors for Fe3+ in aqueous media

Three Rhodamine B derivatives were synthesized and characterized by ESI‐MS, NMR, HR‐MS and IR. The probes exhibit high selectivity and sensitivity towards Fe³⁺ over other metal ions in CH₃CN–water. Upon the addition of Fe³⁺, the spirocyclic ring of the probe was opened and a significant enhancement of visible color and fluorescence within the range of 540–700 nm was observed. The colorimetric and fluorescent response to Fe³⁺ can be conveniently detected even by the naked eye, which provides a facile method for the visual detection of Fe³⁺. Job's plot, fluorescence titration and MS indicated the formation of 1:2 complexes between the probes and Fe³⁺. The reversibility of the reaction establishes the potential of these probes as chemosensors for Fe³⁺ detection. Copyright © 2013 John Wiley & Sons, Ltd.