Branching fractions and CP asymmetries in B0-->pi0pi0, B+-->pi+pi0, and B+-->K+pi0 decays and isospin analysis of the B-->pipi system

Based on a sample of 227 x 10(6) BB pairs collected by the BABAR detector at the PEP-II asymmetric-energy B Factory at SLAC, we measure the branching fraction B(B0-->pi(0)pi(0))=(1.17+/-0.32+/-0.10)x10(-6), and the asymmetry Cpi(0)(pi(0))=-0.12+/-0.56+/-0.06. The B0-->pi(0)pi(0) signal has a significance of 5.0 sigma. We also measure B(B+-->pi(+)pi(0))=(5.8+/-0.6+/-0.4)x10(-6), B(B+-->K+pi(0))=(12.0+/-0.7+/-0.6)x10(-6), and the charge asymmetries Api(+)(pi(0))=-0.01+/-0.10+/-0.02 and AK+(pi(0))=0.06+/-0.06+/-0.01. Using isospin relations, we find an upper bound on the angle difference |alpha-alpha(eff)| of 35 degrees at the 90% C.L.     

Search for radiative penguin decays B(+)-->rho(+)gamma, B(0)-->rho(0)gamma, and B(0)-->omegagamma

A search for the decays B-->rho(770)gamma and B0-->omega(782)gamma is performed on a sample of 211 x 10(6) Upsilon(4S)-->BB events collected by the BABAR detector at the SLAC PEP-II asymmetric-energy e(+)e(-) storage ring. No evidence for the decays is seen. We set the following limits on the individual branching fractions: B(B+-->rho(+)gamma)<1.8 x 10(-6), B(B0-->rho(0)gamma)<0.4 x 10(-6), and B(B0-->omegagamma)<1.0 x 10(-6) at the 90% confidence level. We use the quark model to limit the combined branching fraction B [B-->(rho/omega)gamma]<1.2 x 10(-6), from which we determine a constraint on the ratio of Cabibbo-Kobayashi-Maskawa matrix elements |V(td)|/|V(ts)|.     

Study of a system for introducing metal chelate complexes in AAS

Summary The possibility of extending the sampling of volatile phases in AAS by use of metal beta-diketonates is considered. An electrically heated system was designed in which the chelate was injected, volatilized and then carried by a nitrogen stream to a silica tube, which was heated with an air-acetylene flame. The method was investigated for Cr, Zn and Mn using acetylacetone as chelating agent. The introduction of volatile chelates gives an increase in sensitivity with respect to the nebulization and atomization of solutions in the flame. This sampling system is limited to metallic chelates which are thermally stable and sufficiently volatile. The partial decomposition, which Zn acetyl-acetonate and, particularly Mn acetylacetonate undergo, causes a reduction in the sensitivity and precision of the determination.

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Untersuchung eines Probeeingabesystems für Metallchelatkomplexe in der AASEinfluß der Chelatstabilität

     

Effect of nanoparticle treatment on expression of a key gene involved in thymoquinone biosynthetic pathway in Nigella sativa L.

Thymoquinone is the most important secondary metabolite in black Cumin, which has several pharmaceutical applications. In this study, effect of TiO₂ and SiO₂ nanoparticles as new elicitors, on expression of Geranyl diphosphate synthase gene (GPPS gene), as a key gene involved in thymoquione biosynthesis pathway was investigated in two Iranian accessions. Plants were treatment in the early flowering stage and after 24 h of 50 and 100 mg/L of each nanoparticle, separately. After RNA extraction, GPPS gene expression was analysed by qRT-PCR method. The results showed that the TiO₂ and SiO₂ nanoparticles, generally stimulates the GPPS expression. The TiO₂ nanoparticles were more effective than SiO₂ for the induction of GPPS expression. Also, 100 mg/L treatment of nanoparticles raised gene expression more than 50 mg/L concentration. It can be concluded these nanoparticles can be used as robust elicitors to enhance the production of Thymoquinone in black cumin through up-regulation of related metabolic pathway genes.     

Hydrogen is essential for sustainability

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Fabrication and the electrochemical activation of network-like MnO<Subscript>2</Subscript> nanoflakes as a flexible and large-area supercapacitor electrode

Porous network-like MnO₂ thick films are successfully synthesized on a flexible stainless steel (SS) mesh using a simple and low-cost electrodeposition method followed by an electrochemical activation process. Morphology, chemical composition, and crystal structure of the prepared electrodes before and after the activation process are determined and compared by scanning electron microscopy (SEM), Fourier-transform infrared spectroscopy (FTIR), and X-ray diffraction (XRD) analyses. The results show that the implementation of the electrochemical activation process does not change the chemical composition and crystal structure of the films, but it influences the surface morphology of the MnO₂ thick layer to a flaky nanostructure. Based on the electrochemical data analysis, the maximum specific capacitance of 1400 mF (381 F g^?1) and 3700 mF (352 F g^?1) are measured for small (2.6 cm²) and large (10 cm²) surface area electrodes, respectively. In addition, a flexible symmetric MnO₂//MnO₂ solid-state supercapacitor shows a capacitance of 0.3 F with about 98% retention at different bending angles from 0 to 360°.     

Direct Measurement of Charge Regulation in Metalloprotein Electron Transfer

Determining whether a protein regulates its net electrostatic charge during electron transfer (ET) will deepen our mechanistic understanding of how polypeptides tune rates and free energies of ET (e.g., by affecting reorganization energy, and/or redox potential). Charge regulation during ET has never been measured for proteins because few tools exist to measure the net charge of a folded protein in solution at different oxidation states. Herein, we used a niche analytical tool (protein charge ladders analyzed with capillary electrophoresis) to determine that the net charges of myoglobin, cytochrome c, and azurin change by 0.62±0.06, 1.19±0.02, and 0.51±0.04 units upon single ET. Computational analysis predicts that these fluctuations in charge arise from changes in the pK_a values of multiple non‐coordinating residues (predominantly histidine) that involve between 0.42–0.90 eV. These results suggest that ionizable residues can tune the reactivity of redox centers by regulating the net charge of the entire protein–cofactor–solvent complex.