Dihydrogen activation by a diruthenium analogue of the Fe-only hydrogenase active site

The photochemical reaction of Ru2(S2C3H6)(CO)4(PCy3)2 (1) and H2 gives the dihydride Ru2(S2C3H6)(mu-H)(H)(CO)3(PCy3)2 (2). NMR and crystallographic studies reveal mutually trans basal phosphine ligands and both bridging and terminal hydrides. Ru2(S2C2H4)(CO)4(PCy3)2 behaves similarly. Other HX substrates undergo photoaddition to 1, affording Ru2(S2C3H6)(mu-H)(X)(CO)3(PCy3)2 for X = OTs (3a), Cl (3b), and SPh (3c). Treatment of Ru2(S2C3H6)(mu-H)(H)(CO)3(PCy3)2 with [H(OEt2)]BArF4 (ArF = B(C6H3-3,5-(CF3)2) in CD2Cl2 gives [Ru2(S2C3H6)(mu-H)(CO)3(PCy3)2(H2)]+ (4), which catalyzes H2-D2 exchange. The reaction of 2 with [D(OEt2)]BArF4 gave [Ru2(S2C3H6)(mu-H)(CO)3(PCy3)2(HD)]+ (JH-D = 31 Hz). These studies provide the first models for the Fe-only hydrogenases that bear dihydrogen and terminal hydrido ligands.     

Mikrochemie Physikalische und physikochemische Methoden und Apparate

Ohne Zusammenfassung     

Ethyl methyl 1,4‐dihydro‐4‐(3‐nitrophenyl)‐2,6‐bis(1‐piperidylmethyl)­pyridine‐3,5‐dicarboxylate

In the title compound, C₂₈H₃₈N₄O₆, the 4‐aryl substituent occupies a pseudo‐axial position approximately orthogonal to the plane of the di­hydro­pyridine ring [88.1 (3)°]. The di­hydro­pyridine ring adopts a flattened boat conformation. The H atom on the pyridine N atom is involved in a bifurcated intramolecular hydrogen bond, the acceptors being the N atoms of the two piperidyl­methyl groups [N?N 2.629 (4) and 2.695 (4) Å].     

A complete $\mathcal{O}(\alpha_{\mathrm{S}}^{2})$ calculation of the signal–background interference for the Higgs diphoton decay channel

We analyze a noncommutative model of BTZ spacetime based on deformation of the standard symplectic structure of phase space, i.e., a modification of the standard commutation relations among coordinates and momenta in phase space. We find a BTZ-like solution that is nonperturbative in the non-trivial noncommutative structure. It is shown that the use of deformed commutation relations in the modified non-canonical phase space eliminates the horizons of the standard metric.     

Validation of an LC method to determine skin retention profile of genistein from nanoemulsions incorporated in hydrogels

Recent studies have shown the effect of soy isoflavones in preventing skin photoaging and photocarcinogenesis, especially for genistein (GEN). Nanoemulsions have been proposed as a delivery system for GEN administration due to the low water solubility of this isoflavone. This article describes the validation of an isocratic liquid chromatography method to determine GEN in porcine ear skin layers from nanoemulsions before and after incorporation into hydrogels. The analyses are performed on a reversed-phase C18 column using a mobile phase composed of methanol-water (70:30, v/v) under acid conditions (at pH 3.0) and UV detection at 270 nm. The method is linear in the range of 0.1-10 μg/mL (r(2) > 0.999) in the presence of skin extracts. The low limit of quantitation is estimated as 0.1 μg/mL. No interferences from formulation excipients or skin layer compounds are detected. The RSD values for intra- and inter-day precision are lower than 15%. Recovery ranged from approximately 90% to 110%. The method is applied to estimate GEN retention in the skin from formulations using Franz diffusion cells. The highest amount of GEN is detected in the epidermis (185 μg/cm(2)). In conclusion, the method proved to be specific, precise, and accurate in determining GEN amounts from formulations in skin retention studies.     

Quantitation of clobazam in human plasma using high-performance liquid chromatography.

A rapid and simple reversed-phase high-performance liquid chromatographic (HPLC) method for the determination of clobazam concentrations in human blood samples is developed and validated. Solid-phase column extraction is performed to clean up blood samples before running the analytical HPLC system. The chromatography is isocratic with a mobile phase consisting of acetonitrile (20%, v/v), methanol (23%, v/v), and 0.1 M potassium hydrogen phosphate buffer (pH 3.6; 57%, v/v) at a constant flow rate of 2 mL/min. Clobazam is detected at 226 nm. Chromatography is completed within less than 25 min. The recovery rate is greater than 95% and linear over a wide range of drug concentrations. The intra-assay coefficient of variation percentage varies between 4.3 and 12. This method is used for therapeutic drug monitoring in patients undergoing antiepileptic therapy with clobazam. Plasma levels of clobazam ranged from 21 to 663 ng/mL. Other antiepileptic compounds, such as clonazepam and phenobarbital, did not interfere with the detection of clobazam.     

Structural study of highly halogenated dihydropyridine derivatives as potential calcium channel modulators

Two dihydropyridines endowed with fluorine atoms ( 3 ) and fluorine and chlorine atoms ( 4 ) have been synthesized and structurally characterized by experimental X‐ray analyses and theoretical calculations at the semiempirical (AMI) and ab initio (HF/6–31G*) levels. The results show that these compounds meet the required criteria to act as potential calcium channel modulators.     

Casein phosphoproteome: identification of phosphoproteins by combined mass spectrometry and two-dimensional gel electrophoresis

We report a fast and easy-to-use procedure that combines polyacrylamide gel electrophoresis with matrix assisted laser desorption/ionization-time of flight-mass spectrometry (MALDI-TOF) and nanoelectrospray-tandem mass spectrometry (nES-MS/MS) analysis for the identification of casein components and defined phosphorylated sites. This methodology ensured identification of more than 30 phosphorylated proteins, five beta-, fifteen alpha(s1)-, ten alpha(s2)-, and four kappa-casein (CN) components, including nonallelic, differently phosphorylated, and glycosylated forms. The sugar motif covalently bound to kappa-CN was identified as chains, trisaccharide GalNAc, Gal, NeuGc, and tetrasaccharide 1GalNAc, 1Gal, 2NeuGc. Also identified was a biantennary chain made up of both chains of trisaccharide 1GalNAc, 1Gal, 1NeuGc, and tetrasaccharide 1GalNAc, 1Gal, 2NeuGc moiety on a single kappa-CN component. The phosphate group on site Ser12 of tryptic peptide 8-22 of most phosphorylated alpha(s1)-CN (11 phosphate groups) was localized and the oligosaccharide sequence of the main tryptic glycopeptides of two kappa-CN components was determined by means of MS/MS analysis.