2-(1-Propyl-2,6-distyryl-1,4-dihydro­pyridin-4-yl­idene)malononitrile

In the title compound, C27H23N3, the dihedral angles between the central pyridine ring and the two outer benzene rings are 32.6 (1) and 52.0 (1)°. The compound displays inter­molecular π–π inter­actions between adjacent six-membered rings, the shortest centroid–centroid distance being 3.981 (3) Å

Electronic structure of single-walled carbon nanotubes on ultrathin insulating films

The electronic structures of single-walled carbon nanotubes on Ag(100) and on ultrathin insulating NaCl(100)/Ag(100) were studied using low-temperature scanning tunneling microscopy. The Fermi level of the nanotubes was shifted toward the conduction band on Ag(100), while it was shifted toward the valence band on NaCl films. We explain this opposite behavior by different basic mechanisms accounting for the Fermi level shifts. On the metal surface, the work function difference between the tube and the substrate determines the direction of the Fermi level shift. In the case of carbon nanotubes on insulating films, the electric field resulting from the dipole moment formed at the interface between the insulating film and the metal plays a decisive role in determining the Fermi level.open8

Controlling water dissociation on an ultrathin MgO film by tuning film thickness

Periodic density-functional theory calculations at the single-molecule level were used to study dissociation of water on ultrathin MgO films with varying thickness deposited on the Ag(100) surface. The enhanced chemical activity for water dissociation on MgO/Ag(100) originates from the greater stability of dissociated products, which is due in turn to the strong hybridization of their electronic states at the oxide-metal interface. Our results provide insights into the superiority of the monolayer MgO film surface over the bulk surface and the use of the film thickness to control heterogeneous catalysis in water dissociation.open11

Development of an extension of GeoServer for handling 3D spatial data

Recently, several open source software tools such as CesiumJS and iTowns have been developed for dealing with 3-dimensional spatial data. These tools mainly focus on visualization of 3D spatial data based on WebGL. An open-sourced server capable of storing, sharing and querying 3D spatial data has not yet been developed. GeoServer, one of the representative open source spatial data servers, provides many powerful features. In particular, it supports connecting to and publishing spatial data from a variety of data sources. GeoServer also supports Web Feature Service (WFS), which is a standard protocol established by the Open Geospatial Consortium to request geospatial feature data. However, GeoServer provides functions only for two-dimensional geometry, so it provides few functions for handling 3D spatial data. Because JTS Topology Suite, which is an important component of GeoServer, does not support 3D spatial operations, it also does not support solid geometries. In this paper, we discuss extension modules of GeoServer that we have implemented to handle 3D spatial data. First, instead of JTS, our modules adopted a geometry model based on the ISO 19107 standard and support 3D spatial operations from the Simple Feature CGAL library. Based on this geometry model, we have implemented new internal data structures that represent spatial information from the Feature interface in GeoServer. Second, we also extended the DataStore module to handle and store 3D spatial information for several data sources such as GeoJSON, GML and PostGIS. Finally, we extended the WFS module to share 3D spatial data via GeoServer

Production of biohydrogen by recombinant expression of [NiFe]-hydrogenase 1 in Escherichia coli

<p>Abstract</p> <p>Background</p> <p>Hydrogenases catalyze reversible reaction between hydrogen (H₂) and proton. Inactivation of hydrogenase by exposure to oxygen is a critical limitation in biohydrogen production since strict anaerobic conditions are required. While [FeFe]-hydrogenases are irreversibly inactivated by oxygen, it was known that [NiFe]-hydrogenases are generally more tolerant to oxygen. The physiological function of [NiFe]-hydrogenase 1 is still ambiguous. We herein investigated the H₂production potential of [NiFe]-hydrogenase 1 of <it>Escherichia coli in vivo </it>and <it>in vitro</it>. The <it>hya</it>A and <it>hya</it>B genes corresponding to the small and large subunits of [NiFe]-hydrogenase 1 core enzyme, respectively, were expressed in BL21, an <it>E. coli </it>strain without H₂producing ability.</p> <p>Results</p> <p>Recombinant BL21 expressing [NiFe]-hydrogenase 1 actively produced H₂(12.5 mL H₂/(h·L) in 400 mL glucose minimal medium under micro-aerobic condition, whereas the wild type BL21 did not produce H₂even when formate was added as substrate for formate hydrogenlyase (FHL) pathway. The majority of recombinant protein was produced as an insoluble form, with translocation of a small fraction to the membrane. However, the membrane fraction displayed high activity (~65% of total cell fraction), based on unit protein mass. Supplement of nickel and iron to media showed these metals contribute essentially to the function of [NiFe]-hydrogenase 1 as components of catalytic site. In addition, purified <it>E. coli </it>[NiFe]-hydrogenase 1 using his₆-tag displayed oxygen-tolerant activity of ~12 nmol H₂/(min·mg protein) under a normal aeration environment, compared to [FeFe]-hydrogenase, which remains inactive under this condition.</p> <p>Conclusions</p> <p>This is the first report on physiological function of <it>E. coli </it>[NiFe]-hydrogenase 1 for H₂production. We found that [NiFe]-hydrogenase 1 has H₂production ability even under the existence of oxygen. This oxygen-tolerant property is a significant advantage because it is not necessary to protect the H₂production process from oxygen. Therefore, we propose that [NiFe]-hydrogenase can be successfully applied as an efficient biohydrogen production tool under micro-aerobic conditions.</p

Important predictor of mortality in patients with end-stage liver disease

Prognosis is an essential part of the baseline assessment of any disease. For predicting prognosis of end-stage liver disease, many prognostic models were proposed. Child-Pugh score has been the reference for assessing the prognosis of cirrhosis for about three decades in end-stage liver disease. Despite of several limitations, recent large systematic review showed that Child-Pugh score was still robust predictors and it's components (bilirubin, albumin and prothrombin time) were followed by Child-Pugh score. Recently, Model for end-stage liver disease (MELD) score emerged as a "modern" alternative to Child-Pugh score. The MELD score has been an important role to accurately predict the severity of liver disease and effectively assess the risk of mortality. Due to several weakness of MELD score, new modified MELD scores (MELD-Na, Delta MELD) have been developed and validated. This review summarizes the current knowledge about the prognostic factors in end-stage liver disease, focusing on the role of Child-Pugh and MELD score

Nanotextured Morphology of Poly(methyl methacrylate) and Ultraviolet Curable Poly(urethane acrylate) Blends via Phase Separation

Domain structures of spin-coated immiscible poly(methyl methacrylate) (PMMA) and ultraviolet (UV) curable poly(urethane acrylate) (PUA) blends were studied using atomic force microscopy (AFM). Spin casting the PMMA/PUA blends in propylene glycol monomethyl ether acetate (PGMEA) was accompanied with phase separation, and PUA was subsequently cross-linked under UV radiation. Selective dissolution of PMMA in the phase-separated films was feasible using tetrahydrofuran (THF) solvent after the UV curing process, because the cured PUA material is highly stable against THF. Morphology of phase-separated structure, including domain size and height, could be controlled by varying total concentration of the blended solution, and various nanoscale features such as island-like and hole-like structures were achieved by changing weight ratio of the two immiscible polymers

Improved production of biohydrogen in light-powered Escherichia coli by co-expression of proteorhodopsin and heterologous hydrogenase

<p>Abstract</p> <p>Background</p> <p>Solar energy is the ultimate energy source on the Earth. The conversion of solar energy into fuels and energy sources can be an ideal solution to address energy problems. The recent discovery of proteorhodopsin in uncultured marine γ-proteobacteria has made it possible to construct recombinant <it>Escherichia coli </it>with the function of light-driven proton pumps. Protons that translocate across membranes by proteorhodopsin generate a proton motive force for ATP synthesis by ATPase. Excess protons can also be substrates for hydrogen (H₂) production by hydrogenase in the periplasmic space. In the present work, we investigated the effect of the co-expression of proteorhodopsin and hydrogenase on H₂production yield under light conditions.</p> <p>Results</p> <p>Recombinant <it>E. coli </it>BL21(DE3) co-expressing proteorhodopsin and [NiFe]-hydrogenase from <it>Hydrogenovibrio marinus </it>produced ~1.3-fold more H₂in the presence of exogenous retinal than in the absence of retinal under light conditions (70 μmole photon/(m²·s)). We also observed the synergistic effect of proteorhodopsin with endogenous retinal on H₂production (~1.3-fold more) with a dual plasmid system compared to the strain with a single plasmid for the sole expression of hydrogenase. The increase of light intensity from 70 to 130 μmole photon/(m²·s) led to an increase (~1.8-fold) in H₂production from 287.3 to 525.7 mL H₂/L-culture in the culture of recombinant <it>E. coli </it>co-expressing hydrogenase and proteorhodopsin in conjunction with endogenous retinal. The conversion efficiency of light energy to H₂achieved in this study was ~3.4%.</p> <p>Conclusion</p> <p>Here, we report for the first time the potential application of proteorhodopsin for the production of biohydrogen, a promising alternative fuel. We showed that H₂production was enhanced by the co-expression of proteorhodopsin and [NiFe]-hydrogenase in recombinant <it>E. coli </it>BL21(DE3) in a light intensity-dependent manner. These results demonstrate that <it>E. coli </it>can be applied as light-powered cell factories for biohydrogen production by introducing proteorhodopsin.</p