Silver monoliths and their applications in catalytic reduction of 4-NP to 4-AP and sensing against As3+

Journal of Porous Materials - Silver monoliths using non-ionic surfactant Triton X-102 as reducing agent with and without additives such as Dextran and Ludox (SiNPs) were synthesized by modified...     

Characterization of a site-directed mutant of cytochrome b5 designed to alter axial imidazole ligand plane orientation

Mutants of cytochrome b5 were designed to achieve reorientation of individual axial imidazole ligands. The orientation of the axial ligand planes is thought to modulate the reduction potential of bis(imidazole) axially ligated heme proteins. The A67V mutation achieved this goal through the substitution of a bulkier, hydrophobic ligand for a residue, in the sterically hindered hydrophobic heme binding pocket. Solution structures of mutant and wild-type proteins in the region of the mutation were calculated using restraints obtained from 1H and 15N 2D homonuclear and heteronuclear NMR spectra and 1H-15N 3D heteronuclear NMR spectra. More than 10 restraints per residue were used in the refinement of both structures. Average local rmsd for 20 refined structures was 0.30 A for the wild-type structure and 0.38 A for the A67V mutant. The transfer of amide proton resonance assignments from wild-type to the mutant protein was achieved through overlays of 15N-1H heteronuclear correlation spectra of the reduced proteins. Side chain assignments and sequential assignments were established using conventional assignment strategies. Calculation of the orientation of the components of the anisotropic paramagnetic susceptibility tensor, using methods similar to procedures applied to the wild-type protein, shows that the orientation of the in-plane components are identical in the wild-type and mutant proteins. However, the orientation of the z-component of the susceptibility tensor calculated for the mutant protein differs by 17 degrees for the A-form and by 11 degrees for the B-form from the orientation calculated for the wild-type protein. The rotation of the z-component of the susceptibility tensor (toward the delta meso proton) is in the same direction and is of the same magnitude as the rotation of the H63 imidazole ring induced by mutation.     

Effect of various lipid-bile salt mixed micelles on the intestinal absorption of amphotericin-B in rat

We investigated the effect of the somatosensory functions to the outcomes of motor functions in 28 patients with thalamic hemorrhage. The disturbance of the pyramidal tracts was assessed by the destruction of the internal capsule found in computed tomography (CT). The disturbance of the somatosensory function was analyzed by the N20 component of short-latency somatosensory evoked potentials (SSEP). The outcomes of motor function was evaluated after 3 months of ictus. Correlations between the outcomes of motor function, disturbance of the pyramidal tract, and disturbance of the somatosensory function were discussed. The result indicated that functional outcomes statistically correlated with neither disturbance of the internal capsule alone nor disturbance of N20 alone. But, there was statistically significant between functional outcomes and the combination of disturbance of the internal capsule with disturbance of N20 (p < 0.05, Wilcoxon signed-rank). There was not statistical difference in hematoma volume or consciousness. The implications of these results suggest that somatosensory function may affect the recovery of motor functions.     

Fabrication of silver monoliths using Brij 52 surfactant and TiO2 nanoparticles and their applications to reduce Fast Sulphon Black F dye and sensor against Pb2+

Journal of Materials Science: Materials in Electronics - Silver monoliths were prepared using Brij 52 as surfactant with and without dextran and reinforcing agents TiO2NPs by modified sol–gel...     

Photocatalytic reduction of some alkali carbonates in the presence of methylene blue

The photoreduction of aqueous sodium and potassium carbonates has been carried out in the presence of methylene blue solution (which is a photocatalyst also). The photocatalytic formation of formic acid and formaldehyde were measured spectrophotometrically using Nash reagent. The effect of variation of various parameters like pH, amount of photocatalyst (methylene blue concentration), concentration of Na₂CO₃ and K₂CO₃, light intensity, etc. on the yield of photoproducts was also investigated. A tentative mechanism for this reduction has been proposed. Copyright © 1999 John Wiley & Sons, Ltd.     

Electrochemical Comparison of Heme Proteins by Insulated Electrode Voltammetry

Relatively simple electrochemical probes of redox active proteins can yield a wealth of diverse information concerning their kinetic and thermodynamic reactivity, charge state, and transport rates. In this report, the electrochemical properties of three heme-containing proteins are probed using Au electrodes derivatized with self-assembled monolayers of ω-hydroxyalkanethiols. Cytochrome c and b₅ (wild type from horse and rat, respectively) display low reorganization energies (0.58 eV and 0.44 eV, respectively) and electronic coupling terms which are quite comparable to small redox molecule models. In contrast, metmyoglobin reduction is characterized by a somewhat higher reorganization energy (0.76 eV) and an order of magnitude reduction in its electronic coupling to the electrode. Upon binding oxygen, the reduced oxymyoglobin becomes electroinactive. This radical decrease in the oxymyoglobin redox reactivity is associated with structural and electronic differences caused by the spin-state change induced by oxygen binding. The reactivity differences between these heme-containing proteins are discussed in light of their biochemical function, evolutionary pressures, and structural differences.     

The origin of differences in the physical properties of the equilibrium forms of cytochrome b5 revealed through high-resolution NMR structures and backbone dynamic analyses

On the basis of a comparison of high-resolution solution structures calculated for both equilibrium forms of rat ferrocytochrome b5, differences in reduction potential and thermodyanmic stability have been characterized in terms of significant structural and dynamic differences between the two forms. The dominant difference between A and B conformations has long been known to be due to a 180 degrees rotation of the heme in the binding pocket about an axis defined by the alpha- and gamma-meso carbons, however, the B form has not been structurally characterized until now. The most significant differences observed between the two forms were the presence of a hydrogen bond between the 7-propionate and the S64 amide in the A form but not the B form and surprisingly a displacement of the heme out of the binding pocket by 0.9 A in the B form relative to the A form. The magnitude of other factors which could contribute to the known difference in reduction potentials in the bovine protein [Walker, F. A., Emrick, D., Rivera, J. E., Hanquet, B. J., and Buttlaire, D. H. (1988) J. Am. Chem. Soc. 110, 6234-6240], such as differences in the orientation of the axial imidazoles and differences in hydrogen bond strength to the imidazoles, have been evaluated. The dominant effector of the reduction potential would appear to be the lack of the hydrogen bond to the S64 amide in the B form which frees up the propionate to charge stabilize the iron in the oxidized state and thus lower the reduction potential of the B form. The structure we report for the A form, based on heteronuclear NMR restraints, involving a total of 1288 restraints strongly resembles both the X-ray crystal structure of the bovine protein and a recently reported structure for the A form of the rat protein based on homonuclear data alone [Banci, L., Bertini, I., Ferroni, F., and Rosato, A. (1997) Eur. J. Biochem. 249, 270-279]. The rmsd for the backbone atoms of the A form is 0.54 A (0.92 A for all non-hydrogens). The rmsd for the backbone of the B form is 0.51 A (0. 90 A for all non-hydrogen atoms). An analysis of backbone dynamics based on a model-free analysis of 15N relaxation data, which incorporated axially symmetric diffusion tensor modeling of the cytochrome, indicates that the protein is more rigid in the reduced state relative to the oxidized state, based on a comparison with order parameters reported for the bovine protein in the oxidized state [Kelly, G. P., Muskett, F. W., and Whitford, D. (1997) Eur. J. Biochem. 245, 349-354].     

Tracking Down a New Steroid‐Hydroxylating Promiscuous Cytochrome P450: CYP154C8 from Streptomyces sp. W2233‐SM

CYP154C8 from Streptomyces sp. has been identified as a new cytochrome P450 with substrate flexibility towards different sets of steroids. In vitro treatment of these steroids with CYP154C8 revealed interesting product formation patterns with the same group of steroids. NMR study revealed the major product of corticosterone to be hydroxylated at the C21 position, whereas progesterone, androstenedione, testosterone, and 11‐ketoprogesterone were exclusively hydroxylated at the 16α position. However, the 16α‐hydroxylated product of progesterone was further hydroxylated to yield dihydroxylated products. 16‐hydroxyprogesterone was hydroxylated at two positions to yield dihydroxylated products: 2α,16α‐dihydroxyprogesterone and 6β,16α‐dihydroxyprogesterone. To the best of our knowledge, this is the first report of generation of such products through enzymatic hydroxylation by a CYP450. In view of the importance of modified steroids as pharmaceutical components, CYP154C8 has immense potential for utilization in bioproduction of hydroxylated derivative compounds to be directly employed for pharmaceutical applications.     

Pasting,rheological, and dough mixing behavior of rice flour as affected by the addition of native and partially hydrolyzed β-glucan concentrate

This study was aimed at evaluating the potential of barley β-glucan concentrates (native and partially hydrolyzed) in modifying the techno-functionality of rice flour dough. β-Glucan concentrate was partially hydrolyzed to obtain a low molecular weight polymer and their influence on the pasting, rheological, and thermal properties of rice dough were assessed. Hydration, thermal, and pasting properties were significantly modified with the added β-glucans. The rice dough supplemented with β-glucan concentrates showed improved viscoelastic and creep behavior and the effectiveness of β-glucans in imparting strength to rice dough depended on its molecular weight. Hydrolyzed β-glucan concentrates having low molecular weight increased dough elasticity to the greater extent in comparison to native β-glucan concentrates. The micrographs of supplemented dough showed a strong and dense network indicating improved structure and strength.     

Hydrogen sorption in transition metal exchanged zeolite Y: volumetric measurements and simulation study

Hydrogen adsorption capacities in zeolite Y and its nickel, palladium, rhodium and ruthenium exchanged forms were investigated at 77?K up to 101.3?kPa and 303?K up to 4,000?kPa using a static volumetric adsorption system. Hydrogen adsorption at 77?K for NaY and for Ni, Pd, Rh and Ru exchanged zeolite Y was found to be reversible with pressure. The chemisorption of hydrogen was observed at 303?K for Ni, Pd, Rh and Ru exchanged zeolite Y. Rhodium exchange zeolite Y showed the highest hydrogen adsorption capacity of 1.19 and 0.51 wt% at 77 and 303?K up to 101.3?kpa and 4,000?kpa, respectively. Grand canonical Monte Carlo simulations were also performed to study the adsorption of hydrogen in these zeolites at 77?K as well as 303?K. The simulated adsorption isotherms at 77?K are comparable to experimentally measured isotherms.