The effect of contaminants on the application of polyamine functionalised ion exchange resins for uranium extraction from sulfate based mining process waters

Three in-house produced polyamine functionalised ion exchange resins and Purolite S985 (a commercial ion exchange resin) have been assessed for their ability to extract UO22+ from a variety of aqueous matrices applicable to current and potential future uranium mining processes. The uptake of common contaminant species in uranium processing liquors at variable acid concentrations has been assessed, with Al3+ and MoO42− showing the most extraction, with AsO43−, Eu3+ and Fe3+ showing extractions >10% at low [H+]. Extraction of MoO42−, AsO43−, Eu3+ and Fe3+ was seen to decrease with increasing [H+]. The impact of increasing [Cl−] on UO22+ and Fe3+ extraction has been determined. Fe3+ showed low extractions by all resins, with no dependence on [Cl−]. In contrast, increasing suppression of UO22+ uptake was seen with increasing [Cl−] up to 80 g L−1, with extraction remaining constant beyond this [Cl−]. At high [Cl−] (>50 g L−1) Purolite S985 was seen to remove UO22+ from solution more effectively than all synthesised polyamine resins. The presence of Fe3+ in solution was seen to suppress UO22+ uptake by around 10% when [Fe3+]/[UO22+] increased from 0 to 2. Fe3+ extraction by all studied resins was promoted by the presence of UO22+ in solution. This was most prevalent with Purolite S985, with an extraction of 30% for [Fe3+]/[UO22+] = 2 by Purolite S985. All resins were tested using a process water from a uranium mine and have shown an ability to selectively extract UO22+ from such solutions, with the best synthetic resin recovering 15.7% more uranium than Purolite S985

Promoting Effect of Layered Titanium Phosphate on the Electrochemical and Photovoltaic Performance of Dye-Sensitized Solar Cells

We reported a composite electrolyte prepared by incorporating layered α-titanium phosphate (α-TiP) into an iodide-based electrolyte using 1-ethyl-3-methylimidazolium tetrafluoroborate(EmimBF4) ionic liquid as solvent. The obtained composite electrolyte exhibited excellent electrochemical and photovoltaic properties compared to pure ionic liquid electrolyte. Both the diffusion coefficient of triiodide (I3−) in the electrolyte and the charge-transfer reaction at the electrode/electrolyte interface were improved markedly. The mechanism for the enhanced electrochemical properties of the composite electrolyte was discussed. The highest conversion efficiency of dye-sensitized solar cell (DSSC) was obtained for the composite electrolyte containing 1wt% α-TiP, with an improvement of 58% in the conversion efficiency than the blank one, which offered a broad prospect for the fabrication of stable DSSCs with a high conversion efficiency

Pseudomonas aeruginosa PilY1 Binds Integrin in an RGD- and Calcium-Dependent Manner

PilY1 is a type IV pilus (tfp)-associated protein from the opportunistic pathogen Pseudomonas aeruginosa that shares functional similarity with related proteins in infectious Neisseria and Kingella species. Previous data have shown that PilY1 acts as a calcium-dependent pilus biogenesis factor necessary for twitching motility with a specific calcium binding site located at amino acids 850–859 in the 1,163 residue protein. In addition to motility, PilY1 is also thought to play an important role in the adhesion of P. aeruginosa tfp to host epithelial cells. Here, we show that PilY1 contains an integrin binding arginine-glycine-aspartic acid (RGD) motif located at residues 619–621 in the PilY1 from the PAK strain of P. aeruginosa; this motif is conserved in the PilY1s from the other P. aeruginosa strains of known sequence. We demonstrate that purified PilY1 binds integrin in vitro in an RGD-dependent manner. Furthermore, we identify a second calcium binding site (amino acids 600–608) located ten residues upstream of the RGD. Eliminating calcium binding from this site using a D608A mutation abolished integrin binding; in contrast, a calcium binding mimic (D608K) preserved integrin binding. Finally, we show that the previously established PilY1 calcium binding site at 851–859 also impacts the protein's association with integrin. Taken together, these data indicate that PilY1 binds to integrin in an RGD- and calcium-dependent manner in vitro. As such, P. aeruginosa may employ these interactions to mediate host epithelial cell binding in vivo