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PubMed2002

Crystal structure of the FHA domain of the Chfr mitotic checkpoint protein and its complex with tungstate.

The Chfr mitotic checkpoint protein is frequently inactivated in human cancer. We determined the three-dimensional structure of its FHA domain in its native form and in complex with tungstate, an analog of phosphate. The structures revealed a beta sandwich fold similar to the previously determined folds of the Rad53 N- and C-terminal FHA domains, except that the Rad53 domains were monomeric, whereas the Chfr FHA domain crystallized as a segment-swapped dimer. The ability of the Chfr FHA domain to recognize tungstate suggests that it shares the ability with other FHA domains to bind phosphoproteins. Nevertheless, differences in the sequence and structure of the Chfr and Rad53 FHA domains suggest that FHA domains can be divided into families with distinct binding properties.

Amino Acid Sequence↗

PubMed2002

The memory effect of heteropolyoxotungstate (PM-19) pretreatment on infection by herpes simplex virus at the penetration stage.

The keggin-type heteropolyoxotungstate K(7)[PTi(2)W(10)O(40)].6H(2)O (PM-19) is a potent polyoxometalate (PM) inhibitor of the replication of herpes simplex virus (HSV). Pretreatment of Vero cells with PM-19 prior to HSV-2 infection enhanced the antiviral potency of PM-19 almost 10-fold compared with treatment of the cells only after infection. The pretreatment effect of PM-19 is called "the memory effect". The memory effect was reflected by inhibition of plaque formation and decrease of intracellular virus DNA quantity, and was strongest when PM-19 was present during the penetration stage of HSV-2 infection. The effect was maintained under conditions of fusion induced by polyethyleneglycol treatment. This suggests that PM-19 does not act at the fusion stage of infection. Using the infectious center assay method, it was clarified that a second round of infection was inhibited by about 30% in the presence of PM-19 at the penetration stage compared with the virus control in nontreated cells. The inhibition was enhanced to about 60% by PM-19 pretreatment prior to infection. This suggests that PM-19 pretreatment of the cells protects them against HSV-2 infection.

Animals↗

PubMed2000

A comparison of the effects of two burs on endodontic access in all-ceramic high lucite crowns.

OBJECTIVE: The purpose of this study was to examine and compare the effects of diamond and tungsten carbide burs with respect to the preparation of access through all-ceramic crowns. STUDY DESIGN: Thirty extracted maxillary premolars were restored with all-ceramic crowns. Each specimen was assigned to one of two groups: (1) access opening prepared with a round diamond bur; (2) access opening prepared with a carbide fissure bur. Access preparations were scanned by means of scanning electron microscopy; observed were defects categorized as edge chipping, microcracks, and fractures. RESULTS: Edge chipping around the access was universal. Significant chipping (x > or = 0.1 m) was seen in 43% of access peripheries. Eleven percent of the crowns fractured. chi(2) analysis (P <.05) demonstrated no statistical difference between the bur groups. Results of a t test revealed no statistical difference in edge chipping between the two bur types. CONCLUSIONS: All-ceramic crowns bonded to extracted maxillary premolars may experience edge chipping, microcracks, and fractures at equal rates whether access is prepared with a round medium coarse diamond bur or a tungsten carbide fissure bur.

Bicuspid↗

PubMed2001

Thermal properties and optical transition probabilities of Tm3 + doped TeO2-WO3 glass.

Glasses with the composition of (1 - x)TeO2 + (x)WO3, where x = 0.15, 0.25 and 0.3 were prepared and, their thermal and absorption measurements were carried out. Differential thermal analysis (DTA) curves taken in the 23-600 degrees C temperature range with a heating rate of 10 degrees C/min reveal a change in the value of the glass transition temperature, Tg, while crystallization was not observed for the glasses containing a WO3 content of more than 15 mol%. All the glasses were found to be moisture-resistant. The absorption bands corresponding to the absorption of the 1G4, 3F2, 3F3 and 3F4, 3H5 and 3H4 levels from the 3H6 ground level of the Tm3+ ion were observed in the optical absorption spectra. Integrated absorption cross-sections of each band except that of 3H5 level was found to vary with the glass composition. Judd-Ofelt analysis was carried out for the samples doped with 1.0 mol% Tm2O3. The omega2 parameter shows the strongest dependence on the host composition and it increases with the increasing WO3 amount. The value of omega4 increases rather slowly while the value of omega6 is practically independent of the composition. The strong dependence of the parameter omega2 indicates that this parameter is related to the structural change and the symmetry of the local environment of the Tm3+ ions in this glass.

Differential Thermal Analysis↗

PubMed2002

Determination of total polyphenolic content in red wines by means of the combined He-Ne laser optothermal window and Folin-Ciocalteu colorimetry assay.

The He-Ne laser (632.8 nm) and the concept of optothermal window (OW), a variant of the open photoacoustic cell, were combined with the Folin-Ciocalteu colorimetry assay to quantitate phenolics in four red wines. The total polyphenolic content in selected red wines varied between 786 and 1630 mg/L gallic acid equivalent (GAE) as determined by OW-Folin-Ciocalteu colorimetry, which compares well to 778 and 1614 mg/L GAE obtained for the same wines by means of classical spectrophotometry. The originality and merit of OW colorimetry used here is that, unlike what is encountered in conventional spectrometry, no intermediate dilution step is required when total polyhenolics are determined in red wine. The precision, defined as the closeness to each other of 256 replicate readings of the OW signal, is generally better than 2%.

Colorimetry↗

PubMed1995

Permolybdate and pertungstate--potent stimulators of insulin effects in rat adipocytes: mechanism of action.

In previous studies, tungstate and molybdate were found to mimic the biological actions of insulin. It was suggested that these metallooxides initially inhibit vanadate-sensitive protein phosphotyrosine phosphatase (PTPase). This, in turn, stimulates a staurosporine-sensitive cytosolic protein tyrosine kinase (cytPTK), which activates several insulin bioeffects via insulin-independent pathways (Shisheva & Shechter, 1991, 1993; Elberg et al., 1994). Tungstate and molybdate, however, facilitate bioeffects in rat adipocytes only at high (millimolar) concentrations (Goto et al., 1992). We report here that incubations of tungstate or molybdate with hydrogen peroxide (H2O2) result in the formation of pertungstate (pW, peroxide of tungstate) or permolybdate (pMo, peroxide of molybdate). Pertungstate and permolybdate were found to stimulate all or most of the insulin bioeffects in rat adipocytes. Moreover, these permetallooxides are 80-180-fold more potent stimulators than the corresponding metallooxides. This shift in potency resembles that of pervanadate relative to vanadate in stimulating the same effect in rat adipocytes (Fantus et al., 1989). pW and pMo are also active in normalizing blood glucose levels in streptozotocin-induced diabetic rats. Further studies aimed at understanding the higher efficacy of this permetallooxide revealed the following: (a) All three permetallooxides (pV, pW, pMo) are oxidizing agents relative to reduced glutathione (GSH). They oxidize stoichiometric amounts of GSH to GSSG. (b) All three metallooxides do not oxidize GSH to GSSG. (c) Both metallooxides and permetallooxides inhibit rat adipocytic PTPase at micromolar quantities (IC50 = 3-10 microM). Permetallooxides, however, inhibited a larger PTPase fraction (80-100%) compared to metallooxides (40-70% of the total).(ABSTRACT TRUNCATED AT 250 WORDS)

Adipocytes↗

PubMed2000

The crystal structure of bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily.

Phosphonoacetaldehyde hydrolase (phosphonatase) catalyzes the hydrolysis of phosphonoacetaldehyde to acetaldehyde and phosphate using Mg(II) as cofactor. The reaction proceeds via a novel bicovalent catalytic mechanism in which an active-site nucleophile abstracts the phosphoryl group from the Schiff-base intermediate formed from Lys53 and phosphonoacetaldehyde. In this study, the X-ray crystal structure of the Bacillus cereus phosphonatase homodimer complexed with the phosphate (product) analogue tungstate (K(i) = 50 microM) and the Mg(II) cofactor was determined to 3.0 A resolution with an R(cryst) = 0.248 and R(free) = 0.284. Each monomer is made up of an alpha/beta core domain consisting of a centrally located six-stranded parallel beta-sheet surrounded by six alpha-helices. Two flexible, solvated linkers connect to a small cap domain (residues 21-99) that consists of an antiparallel, five-helix bundle. The subunit-subunit interface, formed by the symmetrical packing of the two alpha8 helices from the respective core domains, is stabilized through the hydrophobic effect derived from the desolvation of paired Met171, Trp164, Tyr162, Tyr167, and Tyr176 side chains. The active site is located at the domain-domain interface of each subunit. The Schiff base forming Lys53 is positioned on the cap domain while tungstate and Mg(II) are bound to the core domain. Mg(II) ligands include two oxygens of the tungstate ligand, one oxygen of the carboxylates of Asp12 and Asp186, the backbone carbonyl oxygen of Ala14, and a water that forms a hydrogen bond with the carboxylate of Asp190 and Thr187. The guanidinium group of Arg160 binds tungstate and the proposed nucleophile Asp12, which is suitably positioned for in-line attack at the tungsten atom. The side chains of the core domain residue Tyr128 and the cap domain residues Cys22 and Lys53 are located nearby. The identity of Asp12 as the active-site nucleophile was further evidenced by the observed removal of catalytic activity resulting from Asp12Ala substitution. The similarity of backbone folds observed in phosphonatase and the 2-haloacid dehalogenase of the HAD enzyme superfamily indicated common ancestry. Superposition of the two structures revealed a conserved active-site scaffold having distinct catalytic stations. Analysis of the usage of polar amino acid residues at these stations by the dehalogenases, phosphonatases, phosphatases, and phosphomutases of the HAD superfamily suggests possible ways in which the active site of an ancient enzyme ancestor might have been diversified for catalysis of C-X, P-C, and P-O bond cleavage reactions.

Amino Acid Sequence↗

PubMed1992

Interaction of porcine uterine fluid purple acid phosphatase with vanadate and vanadyl cation.

Uteroferrin, the purple acid phosphatase from porcine uterine fluid, is noncompetitively inhibited by vanadate in a time-dependent manner under both aerobic and anaerobic conditions. This time-dependent inhibition is observed only with the diiron enzyme and is absent when the FeZn enzyme is used. The observations are attributed to the sequential formation of two uteroferrin-vanadium complexes. The first complex forms rapidly and reversibly, while the second complex forms slowly and results in the production of catalytically inactive oxidized uteroferrin and V(IV), which is observed by EPR. The redox reaction can be reversed by treatment of the oxidized enzyme first with (V(IV)) and then EDTA to generate a catalytically active uteroferrin. Multiple inhibition kinetics suggests that vanadate is mutually exclusive with molybdate, tungstate, and vanadyl cation. The binding site for each of these anions is distinct from the site to which the competitive inhibitors phosphate and arsenate bind. The time-dependent inhibition by vanadate of uteroferrin containing the diiron core represents a new type of mechanism by which vanadium can interact with proteins and gives additional insight into the binding of anions to uteroferrin.

Acid Phosphatase↗

PubMed1983

Effect of oxyanions of the early transition metals on rabbit skeletal muscle phosphorylase.

The differential effects of the oxyanions of the early transition metals ions V(V), W(VI), and Mo(VI) on the catalytic activity and coenzyme binding of rabbit skeletal muscle phosphorylase are studied. The oligoanions of V(V), W(VI), and Mo(VI) are potent inhibitors of phosphorylase. Kinetic studies revealed that oligovanadates inhibit pyridoxal-reconstituted phosphorylase b by competing with both the substrate, glucose 1-phosphate, and the activator, phosphite, with K1 values of 4 microM and 6 microM, respectively. Oligovanadates in the millimolar concentration range inhibit phosphorylases a and b by competing with glucose 1-phosphate binding. The polymeric decavanadate and paratungstates caused time-dependent inactivation of phosphorylase. Spectral studies with tungstate and phosphorylase b revealed that the inactivation is due to deformation of the coenzyme site. Kinetic studies and the protective effects of substrate and effectors on inactivation and deformation by tungstate or vanadate suggest that deformation and inactivation is caused by a primary binding of the oligoanions at the glucose 1-phosphate site. Nuclear magnetic resonance (NMR) studies of vanadate-phosphorylase complexes and vanadate solutions under different conditions were carried out to ascertain the nature of vanadate ions interacting with functional groups in phosphorylase. The results suggest that decavanadate is the major protein-bound species. NMR studies also showed that guanidino groups react with decavanadate and suggest that arginine residues in phosphorylase are potential functional groups that can interact with decavanadate.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

PubMed1988

Inhibition of phosphatase and sulfatase by transition-state analogues.

The inhibition constants for vanadate, chromate, molybdate, and tungstate have been determined with Escherichia coli alkaline phosphatase, potato acid phosphatase, and Helix pomatia aryl sulfatase. Vanadate was a potent inhibitor of all three enzymes. Inhibition of both phosphatases followed the order WO4(2-) greater than MoO4(2-) greater than CrO4(2-). The Ki values for potato acid phosphatase were about 3 orders of magnitude lower than those for alkaline phosphatase. Aryl sulfatase followed the reverse order of inhibition by group VI oxyanions. Phenol enhanced inhibition of alkaline phosphatase by vanadate and chromate but did not affect inhibition of acid phosphatase. Phenol enhanced inhibition of aryl sulfatase by metal oxyanions in all cases following the order H2VO4- greater than CrO4(2-) greater than MoO4(2-) greater than WO4(2-), and N-acetyltyrosine ethyl ester enhanced inhibition of aryl sulfatase by H2VO4- and CrO4(2-) more strongly than did phenol. It is apparent that the effectiveness of metal oxyanions as inhibitors of phosphatases and sulfatases can be selectively enhanced in the presence of other solutes. The relevance of these observations to the effects of transition metal oxyanions on protein phosphatases in vivo is discussed.

Acid Phosphatase↗

PubMed2002

Inhibition of bacteriophage lambda protein phosphatase by organic and oxoanion inhibitors.

Bacteriophage lambda protein phosphatase (lambdaPP) with Mn(2+) as the activating metal cofactor was studied using phosphatase inhibition kinetics and electron paramagnetic resonance (EPR) spectroscopy. Orthophosphate and the oxoanion analogues orthovanadate, tungstate, molybdate, arsenate, and sulfate were shown to inhibit the phosphomonoesterase activity of lambdaPP, albeit with inhibition constants (K(i)) that range over 5 orders of magnitude. In addition, small organic anions were tested as inhibitors. Phosphonoacetohydroxamic acid (PhAH) was found to be a strong competitive inhibitor (K(i) = 5.1 +/- 1.6 microM) whereas phosphonoacetic acid (K(i) = 380 +/- 45 microM) and acetohydroxamic acid (K(i) > 75 mM) modestly inhibited lambdaPP. Low-temperature EPR spectra of Mn(2+)-reconstituted lambdaPP in the presence of oxoanions and PhAH demonstrate that inhibitor binding decreases the spin-coupling constant, J, compared to the native enzyme. This suggests a change in the bridging interaction between Mn(2+) ions of the dimer due to protonation or replacement of a bridging ligand. Inhibitor binding also induces several spectral shifts. Hyperfine splitting characteristic of a spin-coupled (Mn(2+))(2) dimer is most prominent upon the addition of orthovanadate (K(i) = 0.70 +/- 0.20 microM) and PhAH, indicating that these inhibitors tightly interact with the (Mn(2+))(2) form of lambdaPP. These EPR and inhibition kinetic results are discussed in the context of establishing a common mechanism for the hydrolysis of phosphate esters by lambdaPP and other serine/threonine protein phosphatases.

Anions↗

PubMed2005

Characterization of a plant, tyrosine-specific phosphatase of the aspartyl class.

The Arabidopsis thaliana homologue of the Eyes Absent genes (AtEYA) encodes a protein corresponding to the C-terminal conserved domain of the animal Eyes Absent proteins. We show here that AtEYA is a tyrosine-specific phosphatase that hydrolyzes its substrates in a metal-dependent reaction analogous to the phosphoserine phosphatases of the haloacid dehalogenase (HAD) family. The animal Eyes Absent proteins are a novel family of dual-function enzymes: they are transcription factors as well as phosphatases. They also represent a new mechanistic class of tyrosine phosphatases (PTPs) that do not have the Cys-containing signature motif. In contrast, AtEYA is only a tyrosine phosphatase and has no transactivation domain. Using the reaction mechanism of other HAD family enzymes as a model, we have conducted mutational analyses on AtEYA to query the roles of conserved residues. This analysis confirms the importance of the putative nucleophile, the general acid, and the metal-binding residues. Additionally, an inhibitory profile that is diagnostic of this new class of protein tyrosine phosphatases is described. The results of these studies on AtEYA reveal that while the animal and plant Eyes Absent proteins catalyze the same dephosphorylation reaction, the details of their specificity and active site environment, as well as their biological roles, are distinct.

Animals↗

PubMed1998

Extended X-ray absorption fine structure studies of the anion complexes of FeZn uteroferrin.

Molybdate and tungstate are strong inhibitors of the purple acid phosphatases. The binding modes of these anions to the FeZn derivative of uteroferrin, the purple acid phosphatase from porcine uterus (FeZnUf), have been characterized by X-ray absorption spectroscopy at both the iron and zinc K-edges. Pre-edge data show that both FeZnUf.MoO4 and FeZnUf.WO4 have six-coordinate iron sites. Analysis of the EXAFS regions shows that the iron sites of both molybdate and tungstate complexes are best simulated by a shell of three O or N atoms at 2.08-2.09 A and a shell of two O or N atoms at 1.93-1.95 A. On the other hand, the zinc sites have shells of five O or N atoms at approximately 2.1 A and one O or N atom at approximately 2.5 A. Because of the higher resolution of the FeZnUf. MoO4 data, the main shell at approximately 2.1 A can be further split into shells of four O or N at 2.04 A and one O or N at 2.22 A, the latter being associated with a molybdate oxygen. Outer-sphere EXAFS analysis indicates an Fe-Zn separation of approximately 3.4 A for both FeZnUf.MoO4 and FeZnUf.WO4, Fe-Mo/W distances of 3.2 A, and Zn-Mo/W distances of 3.6-3.7 A. Thus, molybdate and tungstate bridge the FeZn active site like phosphate, but do so unsymmetrically. The asymmetric bidentate bridging mode of molybdate and tungstate helps explain the effect of these anions on the redox properties of the diiron uteroferrin.

Acid Phosphatase↗

PubMedDate not supplied

Photodegradation catalyst discovery by high-throughput experiment.

A high-throughput experimental methodology was developed for photocatalysis reaction. In this work, a CCD imaging analysis system and photocatalytic reactor for UV light was designed and tested. By making use of the technologies, we have screened several catalyst libraries. From the SiO2-supported single component catalyst library, we found that TiO2, ZrO2, Nb2O5, and WO3 were good candidates for highly active catalyst formulation. We designed and screened several triangle catalyst libraries and found that the WO3- and Nb2O5-codoped TiO2 catalyst showed much higher photodegradation activities for the degradation of 1,6-hexamethylenediamine than did the pure TiO2 catalyst. The doping of ZrO2 into TiO2 did not generate apparent positive effects on catalytic activity.

Catalysis↗

PubMed2001

Sonolytic, photolytic, and photocatalytic decomposition of atrazine in the presence of polyoxometalates.

Aqueous solutions of atrazine [2-chloro-4-(isopropylamino)-6-(ethylamino)-s-triazine] (CIET) decompose upon illumination with a low-pressure Hg-arc lamp (254 nm). However, no decomposition takes place with lambda > 300 nm. On the other hand, addition of polyoxometalates (POM), PW12O40(3-) or SiW12O40(4-), into a solution of atrazine photodecomposes the substrate within a few minutes (cutoff fiter 320 nm). Ultrasound (US) treatment also decomposes aqueous solutions of atrazine within a few minutes. Both methods, sonolysis and photolysis with POM, give common intermediates, namely, 2-hydroxy-4-(isopropylamino)-6-amino-s-triazine (OIET), 2-chloro-4-(isopropylamino)-6-amino-s-triazine (CIAT), 2-chloro-4-amino-6-(ethylamino)-s-triazine (CAET), 2-hydroxy-4,6-diamino-s-triazine (OAAT), and 2-hydroxy-4-hydroxy-6-amino-s-triazine (OOAT) among others. The final products for both methods, US and photolysis with POM, were cyanuric acid (OOOT), NO3-, Cl-, CO2, and H2O. OOOT showed no signs of decomposition by sonication and/or photolysis with POM. It also resisted degradation upon photolysis with plain UV light (254 nm). However, it has been reported to decompose upon photolysis with lambda > 200 nm. Combination of US and photolysis with POM produces only a cumulative effect.

Atrazine↗

PubMed2001

Investigation of the photocatalytic activity of TiO2--polyoxometalate systems.

The present study reports the investigation of polyoxometalate catalyzed electron transfer from the conduction band of photoexcited TiO2 to molecular oxygen. The oxidation of 1,2-dichlorobenzene (DCB) was used as an index reaction for evaluating the photocatalyst systems TiO2-PW12O40(3-), TiO2-SiW12O40,4- and TiO2-W10O32(4-) in oxygenated aqueous solution. Addition of these polyoxometalate (POM) anions to TiO2 suspensions resulted in significant rate enhancement for DCB oxidation. Photodegradation kinetics exhibited [POM] dependence, experiencing different maximum (k = 0.0318 min(-1), 0.0108 min(-1), and 0.0066 min(-1)) for each POM at different [POM] (0.1 mM PW12O40(3-), 0.07 mM SiW12O40,4- and 1 mM W10O32,4-respectively). The probability that the difference in the adsorption affinity of POMs on TiO2 surface could account for the observed ranking of photodegradation rates was ruled out by adsorption isotherm experiments that revealed similar binding constants for each POM (467 M(-1), 459 M(-1), and 417 M(-1) for PW12O40(3-), SiW12O40(4-), and W10O32(4-), respectively). DCB degradation over TiO2 with O2 or POM+O2 systems can be modeled by the Langmuir-Hinshelwood (saturation kinetics) model. The concentration-independent rate constants (kL-H) for TiO2-O2, TiO2-W10O32(4-), TiO2-SiW12O40(4-), and TiO2-PW12O40(3-) were 0.0818, 0.152, 0.421, and 0.638 min(-1), respectively. An analysis of deltaG for electron transfer from the conduction band of TiO2 to POMs in this study shows that the electron transfer takes place even when it is endothermic.

Absorption↗

PubMed2002

Photocatalytic degradation of aqueous 4-chlorophenol by silica-immobilized polyoxometalates.

The degradation of 4-chlorophenol with near-UV light by silica-immobilized polyoxometalate (POM-in-SiO2) catalysts has been studied. The silica-immobilized Na6W7O24 (SW7), H4W1032 (SW10), H3PW12O40 (SPW12), and H6P2W18O62 (SP2W18) were prepared by means of the sol-gel hydrothermal technique through the hydrolysis of tetraethoxysilane in aqueous solution of the corresponding polyoxometalate, respectively. The degradation of 4-chlorophenol was monitored by measuring Cl- and CO2 concentrations and analyzing reaction intermediates by GC/MS analysis. During irradiation, 4-chlorophenol first dechlorinated to form hydroquinone and p-benzoquinone, and then these intermediates further mineralized to form CO2 and H2O. The degree to which 4-chlorophenol was mineralized by photocatalytic oxidation was investigated. Results indicate less than 15% for SW7 but nearly complete mineralization for SW10 after 60 min of photoirradiation. The present studies suggest that POM-in-SiO2 catalysts may be a novel type of photocatalyts for the purification of the environmentally chlorophenol-contaminated water.

Catalysis↗

PubMed2004

Photocatalysis by titanium dioxide and polyoxometalate/TiO2 cocatalysts. Intermediates and mechanistic study.

A representative polyoxometalate, alpha-12-tungstophosphatic acid (PW12(3-), POM), is loaded on the surface of TiO2 particles used as a cocatalyst to gain further insights into the underlying reaction mechanism and to estimate the feasibility of using the new POM/TiO2 cocatalyst in the photocatalytic degradation of 2,4-dichlorophenol (DCP) in aqueous media. Loading the PW12(3-) species on the surface of TiO2 enhances charge separation in the UV-illuminated TiO2, thereby accelerating the hydroxylation of the initial DCP substrate but not the mineralization of DCP, which is somewhat suppressed in the presence of the polyoxometalate. An increase in the load of POM increases the concentration of aromatic intermediates, and more toxic intermediates, such as 2,6-dichlorodibenzo-p-dioxin, 2,4,6-trichlorophenol, are detected in the PW12(3-)/TiO2 system. By contrast, cleavage of the whole conjugated structure of DCP predominates in TiO2 only dispersions. Strong ESR signals for the superoxide radical anionic species, O2*- (HO2* radicals in acidic media; pH < 5), are detected in TiO2 only dispersions; signals of O2*- are much weaker in the TiO2/ POM composite system under otherwise identical conditions. Experimental results infers that enhancement of charge separation in TiO2 photocatalysis does not always result in improvement of the efficiency of mineralization of organic substrates, and the reaction between organic radical cations and the formed superoxide radical anions may be responsible forthe mineralization of the chlorophenol.

Anthelmintics↗