Chemical and Structural Analysis of Newly Prepared Co-W-Al Alloy by Aluminothermic Reaction

This article is devoted to the characterization of a new Co-W-Al alloy prepared by an aluminothermic reaction. This alloy is used for the subsequent preparation of a special composite nanopowder and for the surface coating of aluminum, magnesium, or iron alloys. Due to the very high temperature (2000 °C–3000 °C) required for the reaction, thermite was added to the mixture. Pulverized coal was also added in order to obtain the appropriate metal carbides (Co, W, Ti), which increase hardness, resistance to abrasion, and the corrosion of the coating and have good high temperature properties. The phase composition of the alloy prepared by the aluminothermic reaction showed mainly cobalt, tungsten, and aluminum, as well as small amounts of iron, titanium, and calcium. No carbon was identified using this method. The microstructure of this alloy is characterized by a cobalt matrix with smaller regular and irregular carbide particles doped by aluminum.

Thermoinduced Structural-transformation and Luminescent Conversion in Hybrid Manganese Halides

We report here the synthesis of hybrid manganese halide crystals, (C4H7N2)MnCl3·H2O and (C4H7N2)2MnCl4, by using the same organic ligand 2-methylimidazole. Upon heating treatment, the red-emissive (C4H7N2)MnCl3·H2O crystal is structurally transformed into green-emissive (C4H7N2)2MnCl4 crystal in situ. The crystal structural analysis reveals that the [MnCl5·H2O]3- octahedra chains decompose into mono [MnCl4]2- tetrahedra, accompanied by the departure of H2O molecules. Upon cooling in air or water vapor, the crystal structure and luminescence of (C4H7N2)2MnCl4 are transformed to those of (C4H7N2)MnCl3·H2O. The in situ conversion of luminescence between (C4H7N2)MnCl3·H2O and (C4H7N2)2MnCl4 provides new insight into the potential application of hybrid manganese halides.

Steric Quenching of Mn(III) Thermal Spin Crossover: Dilution of Spin Centers in Immobilized Solutions

Structural and magnetic properties of a new spin crossover complex [Mn(4,6-diOMe-sal2323)]+ in lattices with ClO4−, (1), NO3−, (2), BF4−, (3), CF3SO3−, (4), and Cl− (5) counterions are reported. Comparison with the magnetostructural properties of the C6, C12, C18 and C22 alkylated analogues of the ClO4− salt of [Mn(4,6-diOMe-sal2323)]+ demonstrates that alkylation effectively switches off the thermal spin crossover pathway and the amphiphilic complexes are all high spin. The spin crossover quenching in the amphiphiles is further probed by magnetic, structural and Raman spectroscopic studies of the PF6− salts of the C6, C12 and C18 complexes of a related complex [Mn(3-OMe-sal2323)]+ which confirm a preference for the high spin state in all cases. Structural analysis is used to rationalize the choice of the spin quintet form in the seven amphiphilic complexes and to highlight the non-accessibility of the smaller spin triplet form of the ion more generally in dilute environments. We suggest that lattice pressure is a requirement to stabilize the spin triplet form of Mn3+ as the low spin form is not known to exist in solution.

Structural and functional analysis of the human Cone-rod homeobox transcription factor

The cone-rod homeobox (CRX) protein is a critical K50 homeodomain transcription factor responsible for the differentiation and maintenance of photoreceptor neurons in the vertebrate retina. Mutant alleles in the human gene encoding CRX result in a variety of distinct blinding retinopathies, including retinitis pigmentosa, cone-rod dystrophy, and Leber congenital amaurosis. Despite the success of using in vitro biochemistry, animal models, and genomics approaches to study this clinically relevant transcription factor over the past 24 years since its initial characterization, there are no high-resolution structures in the published literature for the CRX protein. In this study, we use bioinformatic approaches and small-angle x-ray scattering (SAXS) structural analysis to further understand the biochemical complexity of the human CRX homeodomain (CRX-HD). We find that the CRX-HD is a compact, globular monomer in solution that can specifically bind functional cis-regulatory elements encoded upstream of retina specific genes. This study presents the first structural analysis of CRX, paving the way for a new approach to studying the biochemistry of this protein and its disease-causing mutant protein variants.