Systematic high-pressure synthesis of new filled skutterudites with heavy lanthanide, LnFe4P12 (Ln=heavy lanthanide, including Y)

New filled skutterudites with heavy lanthanide, LnFe₄P₁₂ (Ln=Tb, Dy, Ho, Er, Tm, Yb, Lu and Y) have systematically been prepared for the first time by the high-pressure technique. The relationship between lattice constants and atomic numbers of lanthanide (including Y) is established for LnFe₄P₁₂. Electrical and magnetic properties of several new filled skutterudites with heavy lanthanide have been studied at low temperatures; YFe₄P₁₂ shows a superconducting transition at around 7 K, and DyFe₄P₁₂ behaves as a ferromagnet below 10 K. Electrical and magnetic anomalies in DyFe₄P₁₂ and YFe₄P₁₂ are mainly discussed.     

Noncatalytic kinetic study on site-selective H/D exchange reaction of phenol in sub- and supercritical water

The site-selective H/D exchange reaction of phenol in sub- and supercritical water is studied without added catalysts. In subcritical water in equilibrium with steam at 210-240 degrees C, the H/D exchange proceeds both at the ortho and para sites in the phenyl ring, with no exchange observed at the meta site. The pseudo-first-order rate constants are of the order of 10(-4) s(-1); 50% larger for the ortho than for the para site. In supercritical water, the exchange is observed also at the meta site with the rate constant in the range of 10(-6)-10(-4) s(-1). As the bulk density decreases, the exchange slows down and the site selectivity toward the ortho is enhanced. The enhancement is due to the phenol-water interaction preference at the atomic resolution. The site selectivity toward the ortho is further enhanced when the reaction is carried out in benzene/water solution. Using such selectivity control and the reversible nature of the hydrothermal deuteration/protonation process, it is feasible to synthesize phenyl compounds that are deuterated at any topological combination of ortho, meta, and para sites.     

Plaunol A and B,new anti-ulcer diterpenelactones from Crotonsublyratus

Two new diterpenelactones named plaunol A ($\text{2}$) and B ($\text{3}$) exhibiting anti-Shay ulcer activity were isolated from Thai medicinal plant, $\text{Croton}$$\text{sublyratus}$. Structure of $\text{2}$ was determined by X-ray analysis of its $\text{p}$-bromobenzoate and structure of $\text{3}$ was deduced from the results of chemical correlation and the spectral data.     

Supramolecular assembly based on π-π stacking and π-cation interactions between thiacalix[6]arene and DMF

The molecular assembly of thiacalix[6]arene was formed by π-π stacking and π-DMF interactions between thiacalix[6]arene and adjoining thiacalix[6]arene and between thiacalix[6]arene and DMF, respectively. The X-ray crystal analysis also revealed that hydroxyl groups of thiacalix[6]arene adopted novel two sets of hydrogen bond with two DMF and intramolecular hydrogen bond between phenolic units, which cause to make 1,2,3-alternate configuration structure of thiacalix[6]arene.     

Single crystal EPR studies of the reduced active site of [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F

In the catalytic cycle of [NiFe] hydrogenase the paramagnetic Ni-C intermediate is of key importance, since it is believed to carry the substrate hydrogen, albeit in a yet unknown geometry. Upon illumination at low temperatures, Ni-C is converted to the so-called Ni-L state with markedly different spectroscopic parameters. It is suspected that Ni-L has lost the "substrate hydrogen". In this work, both paramagnetic states have been generated in single crystals obtained from the [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F. Evaluation of the orientation dependent spectra yielded the magnitudes of the g tensors and their orientations in the crystal axes system for both Ni-C and Ni-L. The g tensors could further be related to the atomic structure by comparison with the X-ray crystallographic structure of the reduced enzyme. Although the g tensor magnitudes of Ni-C and Ni-L are quite different, the orientations of the resulting g tensors are very similar but differ from those obtained earlier for Ni-A and Ni-B (Trofanchuk et al. J. Biol. Inorg. Chem. 2000, 5, 36-44). The g tensors were also calculated by density functional theory (DFT) methods using various structural models of the active site. The calculated g tensor of Ni-C is, concerning magnitudes and orientation, in good agreement with the experimental one for a formal Ni(III) oxidation state with a hydride (H(-)) bridge between the Ni and the Fe atom. Satisfying agreement is obtained for the Ni-L state when a formal Ni(I) oxidation state is assumed for this species with a proton (H(+)) removed from the bridge between the nickel and the iron atom.     

Determination of a new cerebral vasodilator 2,6-dimethyl-4-(3-nitrophenyl)-1,4-dihydropyridine-3,5-dicarboxylic acid 3-[2-(N-benzyl-N-methylamino)]-ethyl ester 5-methyl ester hydrochloride (YC-93) in plasma by electron capture gas chromatography

A highly sensitive method for the quantitative determination of 2,6-dimethy-4-(3-nitrophenyl)-1,4-dihydropyridine-3,5-dicarboxylic acid 3-[2-(N-benzyl-N-methyl-amino)]-ethyl ester 5-methyl ester hydrochloride (YC-93) in plasma is described. After extraction, YC-93 was oxidized to pyridine analogue with nitrous acid and detected by electron capture gas chromatography. The sensitivity was 2–3 ng/ml, which is suficient to determine plasma concentrations of YC-93 after oral administration of clinical doses to humans.     

Dual-mode electrochromism switched by proton transfer: dynamic redox properties of bis(diarylmethylenium)-type dyes

Upon oxidative dimerization of pale yellow Ar2C=CHPh 1 (Ar = 4-Me2NC6H4), deep blue 1,4-dication 2(2+) was obtained as a stable salt, which was transformed into 1 by reductive C-C bond fission; deprotonation of 2(2+) gave intense yellow diene 3, which was interconvertible with violet dication 4(2+) by two-electron transfer, thus exhibiting two distinct modes of electrochromism before and after proton transfer.     

Catalytic oxygenative degradation of 4-chlorocatechol by a nonheme iron(III) complex—Mechanism and prevention of catechol ester formation

We examined the oxygenative degradation of 4-chlorocatechol and 4-tert-butylcatechol catalyzed by iron(III)-tris(pyridin-2-yl)amine complex from the standpoint of repressing the formation of 4-chlorocatechol esters of the oxygenated products that causes the incomplete degradation of 4-chlorocatechol. Analysis of the products revealed that 4-chlorocatechol esters are formed by the reaction of muconic anhydride, which is the monooxygenated product, with catechols. It was found that the use of MeOH as the solvent instead of MeCN completely suppressed the catechol ester formation through the methanolysis of muconic anhydride, which greatly improves the degradation efficiency of 4-chlorocatechol.     

Structural regulation of a peptide-conjugated graft copolymer: a simple model for amyloid formation

The self-assembly of peptides and proteins into beta-sheet-rich high-order structures has attracted much attention as a result of the characteristic nanostructure of these assemblies and because of their association with neurodegenerative diseases. Here we report the structural and conformational properties of a peptide-conjugated graft copolymer, poly(gamma-methyl-L-glutamate) grafted polyallylamine (1) in a water-2,2,2-trifluoroethanol solution as a simple model for amyloid formation. Atomic force microscopy revealed that the globular peptide 1 self-assembles into nonbranching fibrils that are about 4 nm in height under certain conditions. These fibrils are rich in beta-sheets and, similar to authentic amyloid fibrils, bind the amyloidophilic dye Congo red. The secondary and quaternary structures of the peptide 1 can be controlled by manipulating the pH, solution composition, and salt concentration; this indicates that the three-dimensional packing arrangement of peptide chains is the key factor for such fibril formation. Furthermore, the addition of carboxylic acid-terminated poly(ethylene glycol), which interacts with both of amino groups of 1 and hydrophobic PMLG chains, was found to obviously inhibit the alpha-to-beta structural transition for non-assembled peptide 1 and to partially cause a beta-to-alpha structural transition against the 1-assembly in the beta-sheet form. These findings demonstrate that the amyloid fibril formation is not restricted to specific protein sequences but rather is a generic property of peptides. The ability to control the assembled structure of the peptide should provide useful information not only for understanding the amyloid fibril formation, but also for developing novel peptide-based material with well-defined nanostructures.