We report the strategy of using the cationic surfactant cetyltrimethylammonium bromide (CTAB) and amino acid L-histidine (His) as co-templates to produce hierarchical ZIF-8 in an aqueous system at room temperature. The hierarchical ZIF-8 had both meso- and microporous structure, resulting in a high mesopore volume as well as specific surface area which can be controlled by the synthesis conditions. We put forward the hypothesis for the formation of a mesoporous structure and the enhancement of the porosity of ZIF-8 that the histidine plays a key role on the stabilization of CTAB micelles and avoiding the production of unexpected by-products therefore promotes the fabrication of pure phase ZIF-8 containing the mesopores interconnected with micropores. The prepared hierarchical ZIF-8 exhibited an excellent performance as a new kind of porous absorbent for efficient removal of the toxic arsenate.

A general one-step in situ pyrolysis route for the construction of metal-organic frameworks encapsulating superparamagnetic γ-Fe2O3NPs dispersed in the confined cavities of MOFs homogeneously is described. The integration of γ-Fe2O3 NPs or clusters into MOFs can endow these porous materials with superparamagnetic element. By the combination of the thermal stability of MOFs and pyrolysis of metal triacetylacetonate complex at matched conditions, the porous structure of MOFs are well maintained while the size-induced superparamagnetic property of nano γ-Fe2O3 is obtained. As a proof of concept, both the γ- Fe2O3@ZIF-8 and γ-Fe2O3@MIL-53(Al) were successfully prepared, and the latter was chosen to demonstrate its potential drug delivery as a magnetic MOF.

Here we present novel (Mg0.2Ti0.2Zn0.2Cu0.2Fe0.2)3O4 materials prepared via one-step solid state reaction method and subsequently high-energy ball-milling. When used as anodes for LIBs, it exhibits superior lithium storage properties.

Recent studies of Saccharomyces cerevisiae revealed sensors that detect extracellular amino acids (Ssy1p) or glucose (Snf3p and Rgt2p) and are evolutionarily related to the transporters of these nutrients. An intriguing question is whether the evolutionary transformation of transporters into nontransporting sensors reflects a homeostatic capability of transporter-like sensors that could not be easily attained by other types of sensors. We previously found SSY1 mutants with an increased basal level of signaling and increased apparent affinity to sensed extracellular amino acids. On this basis, we propose and test a general model for transporter- like sensors in which occupation of a single, central ligand binding site increases the activation energy needed for the conformational shift between an outward-facing, signaling conformation and an inward-facing, nonsignaling conformation. As predicted, intracellular leucine accumulation competitively inhibits sensing of extracellular amino acids. Thus, a single sensor allows the cell to respond to changes in nutrient availability through detection of the relative concentrations of intra- and extracellular ligand.

Amino acids in the environment of Saccharomyces cerevisiae can transcriptionally activate a third of the amino acid permease genes through a signal that originates from the interaction between the extracellular amino acids and an integral plasma membrane protein, Ssy1p. Two plasma membrane-associated proteins, Ptr3p and Ssy5p, participate in the sensing, which results in cleavage of the transcription factors Stp1p and Stp2p, removing 10 kDa of the N terminus of each of them. This confers the transcription factors with the ability to gain access to the nucleus and activate transcription of amino acid permease genes. To extend our understanding of the role of Ptr3p and Ssy5p in this amino acid sensing process, we have isolated constitutive gain-of-function mutants in these two components by using a genetic screening in which potassium uptake is made dependent on amino acid signaling. Mutants which exhibit inducer-independent processing of Stp1p and activation of the amino acid permease gene AGP1 were obtained. For each component of the SPS complex, constitutive signaling by a mutant allele depended on the presence of wild-type alleles of the other two components. Despite the signaling in the absence of inducer, the processing of Stp1p was more complete in the presence of inducer. Dose response assays showed that the median effective concentration for Stp1p processing in the mutant cells was decreased; i.e., a lower inducer concentration is needed for signaling in the mutant cells. These results suggest that the three sensor components interact intimately in a complex rather than in separate reactions and support the notion that the three components function as a complex.

Saccharomyces cerevisiae senses extracellular amino acids using two members of the family of amino acid transporters, Gap1 or Ssy1; aspects of the latter are reviewed here. Despite resemblance with bona fide transporters, Ssy1 appears unable to facilitate transport. Exposure of yeast to amino acids results in Ssy1-dependent transcriptional induction of several genes, in particular some encoding amino acid transporters. Amino acids differ strongly in their potency, leucine being the most potent one known. Using a selection system in which potassium uptake was made dependent on amino acid signalling, our laboratory has obtained and described gain-of-function mutations in SSY1. Some alleles conferred inducer-independent signalling; others increased apparent affinity for inducers. These results revealed that amino acid transport is not required for signalling and support the notion that sensing by Ssy1 occurs via its direct interaction with extracellular amino acids. Current work includes development of quantitative assays of sensing. We use the finding by Per Ljungdahl's laboratory that the signal transduction from Ssy1 involves proteolytic removal of an inhibitory part of the transcriptional activator Stp1. Protein-A Z-domain fused to the C-terminus of Stp1 and Western analysis using antibody against horseradish peroxidase allow quantification of sensing.

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Ultrafine crystalline materials have been extensively investigated as high-rate lithium-storage materials due to their shortened charge-transport length and high surface area. The pseudocapacitive effect plays a considerable role in electrochemical lithium storage when the electrochemically active materials approach nanoscale dimensions, but this has received limited attention. Herein, a series of (Mg 0.2 Co 0.2 Ni 0.2 Cu 0.2 Zn 0.2 )O electrodes with different particle sizes were prepared and tested. The ultrafine (Mg 0.2 Co 0.2 Ni 0.2 Cu 0.2 Zn 0.2 )O nanofilm (3-5 nm) anodes show a remarkable rate capability, delivering high specific charge and discharge capacities of 829, 698, 602, 498 and 408 mA h g À1 at 100, 200, 500, 1000 and 2000 mA g À1 , respectively, and a dominant pseudocapacitive contribution as high as 90.2% toward lithium storage was revealed by electrochemical analysis at a high scanning rate of 1.0 mV s À1 . This work offers an approach to tune the lithium-storage properties of (Mg 0.2 Co 0.2 Ni 0.2 Cu 0.2 Zn 0.2 )O by size control and gives insights into the enhancement of pseudocapacitance-assisted lithium-storage capacity.