Catalytic properties of nanofibrous carbon in selective oxidation of hydrogen sulphide

Nanofibrous carbonaceous materials (NFC) as a new class of materials having many applications, can catalyze the selective oxidation of H2S to sulfur. The correlation between NFC structure and its activity and selectivity in H2S oxidation was determined. It is demonstrated that selectivity can be improved if NFC with more ordered structure be synthesized and the portion of the original catalyst in carbon be reduced by increasing the carbon accumulated in the catalyst.

Sequence-dependent structure/function relationships of catalytic peptide-enabled gold nanoparticles generated under ambient synthetic conditions

Peptide-enabled nanoparticle (NP) synthesis routes can create and/or assemble functional nanomaterials under environmentally friendly conditions, with properties dictated by complex interactions at the biotic/abiotic interface. Manipulation of this interface through sequence modification can provide the capability for material properties to be tailored to create enhanced materials for energy, catalysis, and sensing applications. Fully realizing the potential of these materials requires a comprehensive understanding of sequence-dependent structure/function relationships that is presently lacking. In this work, the atomic-scale structures of a series of peptide-capped Au NPs are determined using a combination of atomic pair distribution function analysis of high-energy X-ray diffraction data and advanced molecular dynamics (MD) simulations. The Au NPs produced with different peptide sequences exhibit varying degrees of catalytic activity for the exemplar reaction 4-nitrophenol reduction. The experimentally derived atomic-scale NP configurations reveal sequence-dependent differences in structural order at the NP surface. Replica exchange with solute-tempering MD simulations are then used to predict the morphology of the peptide overlayer on these Au NPs and identify factors determining the structure/catalytic properties relationship. We show that the amount of exposed Au surface, the underlying surface structural disorder, and the interaction strength of the peptide with the Au surface all influence catalytic performance. A simplified computational prediction of catalytic performance is developed that can potentially serve as a screening tool for future studies. Our approach provides a platform for broadening the analysis of catalytic peptide-enabled metallic NP systems, potentially allowing for the development of rational design rules for property enhancement.

Synthesis and growth of hematite nanodiscs through a facile hydrothermal approach

This study reports a facile hydrothermal method for the synthesis of monodispersed hematite (α-Fe2O3) nanodiscs under mild conditions. The method has features such as no use of surfactants, no toxic precursors, and no requirements of high-temperature decomposition of iron precursors in non-polar solvents. By this method, α-Fe2O3 nanodiscs were achieved with diameter of 50 ± 10 nm and thickness of ~6.5 nm by the hydrolysis of ferric chloride. The particle characteristics (e.g., shape, size, and distribution) and functional properties (e.g., magnetic and catalytic properties) were investigated by various advanced techniques, including TEM, AFM, XRD, BET, and SQUID. Such nanodiscs were proved to show unique magnetic properties, i.e., superparamagnetic property at a low temperature (e.g., 20 K) but ferromagnetic property at a room temperature (~300 K). They also exhibit low-temperature (<623 K) catalytic activity in CO oxidation because of extremely clean surfaces due to non-involvement of surfactants, compared with those spheres and ellipsoids capped by PVP molecules.

High N-content holey few-layered graphene electrocatalysts: Scalable solvent-less production

Few layered nitrogen doped graphene (NG) attracts great interest in energy storage and conversion applications due to its electronic and catalytic properties. However, its bulk production cannot be envisioned by the current synthetic methods. Here we report a facile, solvent-less, low cost and high yield process for the synthesis of NG. Mechanochemical solid-state exfoliation allows scalable synthesis of holey and crumple nitrogen-doped few-layered graphene from graphite with controlled high concentration N doping and a high surface area through ball-milling. By adjusting the ratio of starting materials, the nitrogen content can be modulated from 4.87 to 17.83 at.%. Furthermore, the types of nitrogen-containing species in few-layered graphene can also be controlled. The resultant NG exhibits superior oxygen reduction reaction performance and more reliable stability than commercial Pt/C catalysts. This journal is

Insulin-regulated aminopeptidase : analysis of peptide substrate and inhibitor binding to the catalytic domain

Peptide inhibitors of insulin-regulated aminopeptidase (IRAP) accelerate spatial learning and facilitate memory retention and retrieval by binding competitively to the catalytic site of the enzyme and inhibiting its catalytic activity. IRAP belongs to the M1 family of Zn2+-dependent aminopeptidases characterized by a catalytic domain that contains two conserved motifs, the HEXXH(X)18E Zn2+-binding motif and the GXMEN exopeptidase motif. To elucidate the role of GXMEN in binding peptide substrates and competitive inhibitors, site-directed mutagenesis was performed on the motif. Non-conserved mutations of residues G428, A429 and N432 resulted in mutant enzymes with altered catalytic activity, as well as divergent changes in kinetic properties towards the synthetic substrate leucine β-naphthalamide. The affinities of the IRAP inhibitors angiotensin IV, Nle1-angiotensin IV, and LVV-hemorphin-7 were selectively decreased. Substrate degradation studies using the in vitro substrates vasopressin and Leu-enkephalin showed that replacement of G428 by either D, E or Q selectively abolished the catalysis of Leu-enkephalin, while [A429G]IRAP and [N432A]IRAP mutants were incapable of cleaving both substrates. These mutational studies indicate that G428, A429 and N432 are important for binding of both peptide substrates and inhibitors, and confirm previous results demonstrating that peptide IRAP inhibitors competitively bind to its catalytic site.