A theoretical study on the gas phase reactions of the anions NbO3-, NbO5-, and NbO2(0H)(2)(-) with H2O and O-2

The potential energy surfaces at the singlet (s) and the triplet (t) electronic states associated with the gas-phase ion/molecule reactions of NbO3-, NbO5-, and NbO2(OH)(2)(-) with H2O and O-2 have been investigated by means of DFT calculations at the B3LYP level. An analysis of the results points out that the most favorable reactive channel comprises s-NbO3- reacting with H2O to give an ion-molecule complex s-NbO3(H2O)without a barrier. From this minima, an intramolecular hydrogen transfer takes place between the incoming water molecule and an oxygen atom of the NbO3- fragment to render the most stable minimum, s-NbO2(OH)(2)(-). This oxyhydroxide system reacts with O-2 along a barrierless process to obtain the triplet t-NbO4(OH)(2)(-)-A intermediate, and the crossing point, CP1, between s and t electronic states has been characterized. The next step is the hydrogen-transfer process between the oxygen atom of a hydroxyl group and the one adjacent oxygen atom to render a minimum with the two OH groups near each other, t-NbO4(OH)(2)(-)-B. From this point, the last hydrogen migration takes place, to obtain the product complex, t-NbO5(H2O)(-), that can be connected with the singlet separated products, s-NbO5- and H2O. Therefore, a second crossing point, CP2, has been localized. The nature of the chemical bonding of the key minima (NbO3-, NbO2(OH)(2)(-), NbO4(OH)(2)(-)-B, and NbO5-) in both electronic states of the reaction and an interaction with O-2 has been studied by topological analysis of Becke-Edgecombe electron-localization function (ELF) and atoms-in-molecules (AIM) methodology. The niobium-oxygen interactions are characterized as unshared-electron (ionic) interactions and some oxygen-oxygen interactions as protocovalent bonds.

Preliminary X-ray crystallographic studies of BthTX-II, a myotoxic Asp49-phospholipase A(2) with low catalytic activity from Bothrops jararacussu venom

For the first time, a complete X-ray diffraction data set has been collected from a myotoxic Asp49-phospholipase A(2) (Asp49-PLA(2)) with low catalytic activity (BthTX-II from Bothrops jararacussu venom) and a molecular-replacement solution has been obtained with a dimer in the asymmetric unit. The quaternary structure of BthTX-II resembles the myotoxin Asp49-PLA(2) PrTX-III (piratoxin III from B. pirajai venom) and all non-catalytic and myotoxic dimeric Lys49-PLA(2)s. In contrast, the oligomeric structure of BthTX-II is different from the highly catalytic and non-myotoxic BthA-I (acidic PLA(2) from B. jararacussu). Thus, comparison between these structures should add insight into the catalytic and myotoxic activities of bothropic PLA(2)s.

Crystal structure of a myotoxic Asp49-phospholipase A(2) with low catalytic activity: Insights into Ca2+ -independent catalytic mechanism

A myotoxic Asp49-phospholipase A(2) (Asp49-PLA(2)) with low catalytic activity (BthTX-II from Bothrops jararacussu venom) was crystallized and the molecular-replacement solution has been obtained with a dimer in the asymmetric unit. The quaternary structure of BthTX-II resembles the myotoxic Asp49-PLA2 PrTX-III (piratoxin III from B. pirajai venom) and all non-catalytic and myotoxic dimeric Lys49-PLA(2)s. Despite of this, BthTX-II is different from the highly catalytic and non-myotoxic BthA-I (acidic PLA(2) from B. jararacussu) and other Asp49-PLA(2)s. BthTX-II structure showed a severe distortion of calcium-binding loop leading to displacement of the C-terminal region. Tyr28 side chain, present in this region, is in an opposite position in relation to the same residue in the catalytic activity Asp49-PLA(2)s, making a hydrogen bond with the atom 0 delta 2 of the catalytically active Asp49, which should coordinate the calcium. This high distortion may also be confirmed by the inability of BthTX-II to bind Na+ ions at the Ca2+-binding loop, despite of the crystallization to have occurred in the presence of this ion. In contrast, other Asp49-PLA(2)s which are able to bind Ca2+ ions are also able to bind Na+ ions at this loop. The comparison with other catalytic, non-catalytic and inhibited PLA(2)s indicates that the BthTX-II is not able to bind calcium ions; consequently, we suggest that its low catalytic function is based on an alternative way compared with other PLA(2)s. (c) 2008 Elsevier B.V All rights reserved.

Cycloaddition reaction of the azido-bridged cyclometallated complex [Pd(dmba)N-3](2) with CS2. Crystal and molecular structure of DI(mu, N,S-1,2,3,4-thiatriazole-5-thiolate) bis[(N,N-dimethylbenzyl-amine-C-2,N)palladium(II)]

The 1,3-dipolar cycloaddition of carbon disulfide to the coordinated azide in the cyclometallated compound [Pd(dmba)(N-3)](2) (1), dmba = N,N-dimethylbenzylamine, was investigated. The compound obtained di(mu, N,S-1,2,3,4-thiatriazole-5-thiolate)-bis[(N,N-dimethylbenzylamine-C-2,N)palladium(II)] (2), was characterized by IR spectroscopy and X-ray diffraction. Complex (2) is dimeric with the two [Pd(N,N-dimethylbenzylamine)] moieties being connected by the two vicinal bridging N,S-1,2,3,4-thiatriazole-5-thiolate anions in a square-planar coordination for the palladium atoms.

Structure characterization of molecular complexes for non-linear optical materials. II. 1 : 1 complexes of 4-methyl-morpholine-N-oxide (1) and 3-picoline-N-oxide (2) with 2,4,6-trinitrophenol, studied by X-ray, AM1 and DFT calculations

(1) C6H2N3O7- center dot C5H12NO2+, Mr = 346.26, P2(1)/c, a = 7.2356(6), b = 10.5765(9), c = 19.593(2) angstrom, 3 beta=95.101(6)degrees, V = 1493.5(2) angstrom(3), Z = 4, R-1 = 0.0414; (2) C6H2N3O7- center dot C6H8NO+, Mr = 38.24, P2(1)/n, a = 7.8713(5), b = 6.1979(7), c = 28.697(3) angstrom, beta = 90.028(7)degrees, V = 1400.0(2) angstrom(3), Z = 4, R-1 = 0.0416. The packing units in both compounds consist of hydrogen bonded cation-anion pairs. The (hyper)polarizabilities have been calculated for the crystallographic and optimized molecules, by AM1 and at the DFT/B3LYP(6-31G**) level.

Quenching of para-H-2 with an ultracold antihydrogen atom (H)over-bar(1s)

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Structures of the noncovalent complexes of human and bovine prothrombin fragment 2 with human PPACK-thrombin

Both human and bovine prothrombin fragment 2 (the second kringle) have been cocrystallized separately with human PPACK (D-Phe-Pro-Arg)-thrombin, and the structures of these noncovalent complexes have been determined and refined (R = 0.155 and 0.157, respectively) at 3.3-Å resolution using X-ray crystallographic methods. The kringles interact with thrombin at a site that has previously been proposed to be the heparin binding region. The latter is a highly electropositive surface near the C-terminal helix of thrombin abundant in arginine and lysine residues. These form salt bridges with acidic side chains of kringle 2. Somewhat unexpectedly, the negative groups of the kringle correspond to an enlarged anionic center of the lysine binding site of lysine binding kringles such as plasminogens K1 and K4 and TPA K2. The anionic motif is DGDEE in prothrombin kringle 2. The corresponding cationic center of the lysine binding site region has an unfavorable Arg70Asp substitution, but Lys35 is conserved. However, the folding of fragment 2 is different from that of prothrombin kringle 1 and other kringles: the second outer loop possesses a distorted two-turn helix, and the hairpin β-turn of the second inner loop pivots at Val64 and Asp70 by 60°. Lys35 is located on a turn of the helix, which causes it to project into solvent space in the fragment 2-thrombin complex, thereby devastating any vestige of the cationic center of the lysine binding site. Since fragment 2 has not been reported to bind lysine, it most likely has a different inherent folding conformation for the second outer loop, as has also been observed to be the case with TPA K2 and the urokinase kringle. The movement of the Val64-Asp70 β-turn is most likely a conformational change accompanying complexation, which reveals a new heretofore unsuspected flexibility in kringles. The fragment 2-thrombin complex is only the second cassette module-catalytic domain structure to be determined for a multidomain blood protein and only the third domain-domain interaction to be described among such proteins, the others being factor Xa without a Gla domain and Ca2+ prothrombin fragment 1 with a Gla domain and a kringle. © 1993 American Chemical Society.

Treatment of experimental periodontal disease by a selective inhibitor of cyclooxygenase-2 with scaling and root planing (SRP)

Lumiracoxib is a selective inhibitor of cyclooxygenase-2 (COX-2) approved for the relief of symptoms of chronic inflammatory conditions. The aim of this study was to evaluate the effects of this specific inhibitor of COX-2 as adjunctive treatment on induced periodontitis in rats. Periodontal disease was induced at the first mandibular molar of 60 rats. After 7 days, the ligature was removed and all animals were submitted to scaling and root planing (SRP) along with local irrigation with saline solution and were divided into 2 groups: SRP (n = 30)-received subcutaneous injections of 1 mg/kg of body weight/day of saline solution for 3 days and; SRP + L (n = 30)-received subcutaneous injections of 1 mg/kg of body weight/day of Lumiracoxib for 3 days. Ten animals in each group were killed at 7, 15, and 30 days. The histological description was performed and the histometric values were statistically analyzed. In Group SRP + L, the histometric analysis (0.58 ± 0.08, 0.64 ± 0.06, and 0.56 ± 0.10 mm 2) showed less bone loss (p < 0.05) than Group SRP (1.52 ± 0.08, 1.55 ± 0.09, and 1.49 ± 0.24 mm 2) at 7, 15, and 30 days, respectively. Within the limits of this study it can be concluded that subcutaneous application of specific inhibitor of COX-2 was a beneficial adjunctive treatment for periodontal diseases induced in rats. © 2010 Springer Basel AG.

REACTIONS OF MERCURIC ACETATE WITH PENTACARBONYLIRON IN ALCOHOLS - CRYSTAL AND MOLECULAR-STRUCTURES OF HG[FE(COOR)(CO)(4)](2) (R=CH3, C2H5)

Reactions of Hg(CH3COO)(2) with [Fe(CO)(5)] in MeOH and EtOH lead to the compounds Hg[Fe(COOR)(CO)(4)](2) (I for R = CH3 and II for R = C2H5). Crystals of I are triclinic, P (1) over bar, with a = 6.272(2), b = 6.441(3), c = 11.703(4) Angstrom, a = 92.94(3)degrees, beta = 103.77(3)degrees, gamma = 96.10(2)degrees, and Z = 1. Crystals of II are tetragonal, I4(1)/a, with a = 17.906(3) Angstrom, c = 12.756(2) Angstrom, and Z = 8. The geometry around Hg is linear for compound I and approximately linear for compound II. The Hg-Fe distances are 2.5716(8) and 2.575(4) Angstrom for compounds I and II, respectively. The geometry around the Fe in both compounds is approximately octahedral. The carboalkoxy group is cis to Hg in both compounds with Fe-C distances equal to 2.034(6) and 2.05(4) Angstrom for compounds I and II, respectively.

Cleavage of the dimeric cyclopalladated [Pd(N,C-dmba)(mu-X)](2), (dmba = N,N-dimethylbenzylamine; X = SCN and NCO) by diphosphines. Palladium(II) compounds with distinct structures in the solid-state and in solution

The reactions of the pseudohalide-bridged dimer [Pd(N,C-dmba)(mu -SCN)](2) (1) (dmba = N,N-dimethylbenzylamine) with cis-Ph2PCH=CHPPh2 (cis-dppet) (1:1 molar ratio) and of [Pd(N,C-dmba)(mu -NCO)](2) (2) with Ph2PCH2CH2PPh2 (dppe) (1:2 molar ratio) gave mononuclear [Pd(C-dmba)(SCN)(cis-dppet)].H2O (1a) and [Pd(C-dmba)(NCO)(dppe)] (2a), respectively, with the diphosphines acting as chelating ligands. Reaction of (2) with Fe(C5H4PPh2)(2) (dppf) (1:1 molar ratio) yielded [{Pd(N,C-dmba)(NCO)}(2)(mu -dppf)] (2b), a bimetallic species containing two palladium atoms bridged by the diphosphine, whereas reaction in a 1:2 molar ratio gave the mononuclear [Pd(N,C-dmba)(dppf)][NCO]. CH2Cl2 (2c), with the diphosphine acting as a chelating ligand. The compounds have been characterized by elemental analysis, i.r., P-31{H-1}, C-13- and H-1-n.m.r. spectroscopies. Conductivity measurements together with spectroscopic data showed that (1a) and (2a) do not have the same structure in the solid state and in MeCl solution, whereas for compounds (2b) and (2c) no structural changes were observed when the solids were dissolved in MeCl.

Effects of morin on snake venom phospholipase A(2) (PLA(2))

Flavonoids are potent anti-inflammatory compounds isolated from several plant extracts, and have been used experimentally against inflammatory processes. In this work, a PLA(2) isolated from the Crotalus durissus cascavella venom and rat paw oedema were used as a model to. study the effect of flavonoids on PLA(2). We observed that a treatment of PLA(2) with morin induces several modifications in the aromatic amino acids, with accompanying changes in its amino acid composition. In addition, results from circular dichroism spectroscopy and UV scanning revealed important structural modifications. Concomitantly, a considerable decrease in the enzymatic and antibacterial activities was observed, even though anti-inflammatory and neurotoxic activities were not affected. These apparent controversial results may be an indication that PLA(2) possess a second pharmacological site which does not affect or depend on the enzymatic activity. (c) 2005 Elsevier Ltd. All rights reserved.

Biological and structural characterization of a new PLA(2) from the Crotalus durissus collilineatus venom

In the present article we report on the biological characterization and amino acid sequence of a new basic Phospholipases A(2) (PLA(2)) isolated from the Crotalus durissus collilineatus venom (Cdcolli F6), which showed the presence of 122 amino acid residues with a pI value of 8.3, molecular mass of 14 kDa and revealed an amino acid sequence identity of 80% with crotalic PLA(2)s such as Mojave B, Cdt F15, and CROATOX. This homology, however, dropped to 50% if compared to other sources of PLA(2)s such as from the Bothrops snake venom. Also, this PLA(2) induced myonecrosis, although this effect was lower than that of BthTx-I or whole crotoxin and it was able to induce a strong blockage effect on the chick biventer neuromuscular preparation, independently of the presence of the acid subunid (crotapotin). The neurotoxic effect was strongly reduced by pre-incubation with heparin or with anhydrous acetic acid and rho-BPB showed a similar reduction. The rho-BPB did not reduce significantly the myotoxic activity induced by the PLA(2), but the anhydrous acetic acid treatment and the pre-incu-bation of PLA(2) with heparin reduced significantly its effects. This protein showed a strong antimicrobial activity against Xanthomonas axonopodis passiflorae (Gram-negative), which was drastically reduced by incubation of this PLA(2) with rho-BPB, but this effect was marginally reduced after treatment with anhydrous acetic acid. Our findings here allow to speculate that basic amino acid residues on the C-terminal and molecular regions near catalytic site regions such as Calcium binding loop or rho-wing region may be involved in the binding of this PLA(2) to the molecular receptor to induce the neurotoxic effect. The bactericidal effect, however, was completely dependent on the enzymatic activity of this protein.

Application of the Potentiometric Stripping Analysis with Constant Current for the Determination of Lithium Ions Using a Spinel-Type Manganese (IV) Oxide-Modified Carbon Paste Electrode

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