Search

A new kind of dual-band and high gain waveguide slot antenna is designed in this paper. By combining a folded plate and a double-layer metal structure with four apertures on its top floor, the proposed antenna has a dual-band characteristic and its gain reaches up to 11.9 dB with only 35 degrees (HPBW) of E-plane at 12.7 GHz and 12.1 dB with 39 degrees at 15.0 GHz. Compared to the conventional single-aperture flat antenna, the simulated and measured results show that the proposed antenna with resonant cavity achieves better impedance matching and low profile, meanwhile, the gain improved almost 5.2 dB at 12.7 GHz and 6 dB at 15.0 GHz, the HPBW of E-plane is reduced by 100 degrees and 108 degrees respectively.

Antimony selenide (Sb2Se3) is regarded as one of the key alternative absorber materials for conventional thin film solar cells due to its excellent optical and electrical properties. Here, we proposed a Sb2Se3 thin film solar cell fabricated using a two-step process magnetron sputtering followed by a post-selenization treatment, which enabled us to optimize the best quality of both the Sb2Se3 thin film and the Sb2Se3/CdS heterojunction interface. By tuning the selenization parameters, a Sb2Se3 thin film solar cell with high efficiency of 6.06% was achieved, the highest reported power conversion efficiency of sputtered Sb2Se3 planar heterojunction solar cells. Moreover, our device presented an outstanding open circuit voltage (VOC) of 494 mV which is superior to those reported Sb2Se3 solar cells. State and density of defects showed that proper selenization temperature could effectively passivate deep defects for the films and thus improve the device performance.

Phospholipid-hydroperoxide glutathione peroxidase (PHGPx or GPx4; EC 1.11.1.12) is an antioxidant enzyme that reduces lipid hydroperoxides in biomembranes. Here, we cloned and characterized cys-PHGPx from the bumblebee Bombus ignitus (Bi-PHGPx). The Bi-PHGPx gene consists of 4 exons, encoding 168 amino acid residues with a canonical cys-codon at residue 45 and active site residues Gln(82) and Trp(134). Recombinant Bi-PHGPx, expressed as a 19 kDa protein in baculovirus-infected insect cells, exhibited enzymatic activity against PLPC-OOH and H(2)O(2) using glutathione as an electron donor. Tissue distribution analyses showed the presence of Bi-PHGPx in all tissues examined. Bi-PHGPx transcripts were upregulated by stresses, such as wounding, H(2)O(2) exposure, external temperature shock, and starvation. Under H(2)O(2) overload, the RNA interference (RNAi)-induced thioredoxin peroxidase (BiTPx1)-knock-down B. ignitus worker bees showed upregulated expression of Bi-PHGPx in the fat body. These results indicate that Bi-PHGPx is a stress-inducible antioxidant enzyme that acts on phospholipid hydroperoxide and H(2)O(2).

We previously reported that the beta-1,4-endoglucanase (EGase) belonging to glycoside hydrolase family 45 cloned from the mulberry longicorn beetle, Apriona germari (Ag-EGase I), is composed of 237 amino acid residues and has a potential N-glycosylation site at 97-100 amino acid residues (NSTF). We here describe the N-glycosylation and its role for enzymatic activity of the Ag-EGase I. The N-glycosylation of Ag-EGase I was revealed by the treatment of tunicamycin to the recombinant virus-infected insect Sf9 cells and by endoglycosidase F to the purified recombinant Ag-EGase I, demonstrating that the carbohydrate moieties are not necessary for secretion but essential for Ag-EGase I enzyme activity. To further elucidate the functional role of the N-glycosylation in Ag-EGase I, we have assayed the cellulase enzyme activity in Thr99Gln mutant. Lack of N-glycosylation in Ag-EGase I showed no substantial enzyme activity. This result demonstrates that N-glycosylation at site 97-100 amino acid residues (NSTF) is essential for enzyme activity.