Characterization of airborne carbonate over a site near Asian dust source regions during spring 2002 and its climatic and environmental significance

IEECAS SKLLQG

Identifying paleoflood deposits archived in Zhongba Site, the Three Gorges reservoir region of the Yangtze River, China

IEECAS SKLLQG

The reaction route and active site of catalytic decomposition of hydrazine over molybdenum nitride catalyst

The catalytic properties of the passivated, reduced passivated, and fresh bulk molybdenum nitride for hydrazine decomposition were evaluated in a microreactor. The reaction route of hydrazine decomposition over molybdenum nitride catalysts seems to be the same as that of Ir/gamma-Al2O3 catalysts. Below 673 K, the hydrazine decomposes into N-2 and NH3. Above 673 K, the hydrazine decomposes into N-2 and NH3 first, and then the produced NH3 further dissociates into N-2 and H-2. From the in situ FT-IR spectroscopy, hydrazine is adsorbed and decomposes mainly on the Mo site of the Mo2N/gamma-Al2O3 catalyst. (C) 2004 Elsevier Inc. All rights reserved.

Active site structure of NO decomposition on perovskite(-like) oxides: An investigation from experiment and density functional theory

Active site structure for NO decomposition carried out on perovskite-like oxides were discussed based on the N-2 yield measured from LaSrNi1-x,AlxO4 with different B-site cations and from La2-ySryCuO4 with different crystal phases. Results show that the active site contains two oxygen vacancies, two transition metals, and one lattice-oxygen, with the oxygen vacancy locating on the apex of MO6 octahedron, and the lattice oxygen locating between the two transition metals (i.e., M-O-M plane). Density functional theory (DFT) analysis to the structure shows that this new active site is the most active structure for NO adsorbing, and hence, for NO decomposition. The similar trend of the relative energies that are required for the formation of oxygen vacancies with f form (calculated from DFT), the amount of oxygen vacancies, and the activities (N-2 yield) certifies this result further.

Synthesis, crystal structure, and density of (W1-xAlx)C

A new solid solution system of Al in WC, with the stoichiometry of (W1-xAlx)C (x = 0.10, 0.25, 0.50, 0.75, 0.86), has been synthesized by a solid-state reaction between W1-xAlx alloys and carbon at around 1673 K in vacuum. Environment scanning electron microscope, energy- dispersive analysis of X-ray, X-ray photoelectron spectroscopy, and inductively coupled plasma analyses are used to certify the formation of the products. The mechanism of the solid-state reaction is also discussed. (W1-xAlx)C is identified to crystallize in the hexagonal space group P6m2 (No. 187) and belongs to the WC structure type. The atoms of W and Al occupy the same lattice site (la site) in the cell of (W1-xAlx)C. The cell parameters for each specimen in the phase of W-AI-C are quite close to that of WC, while their densities are far lower than that of WC.

Enthalpy/entropy compensation: Influence of DNA flanking sequence on the binding of 7-amino actinomycin D to its primary binding site in short DNA duplexes

The effect of the context of the flanking sequence on ligand binding to DNA oligonucleotides that contain consensus binding sites was investigated for the binding of the intercalator 7-amino actinomycin D. Seven self-complementary DNA oligomers each containing a centrally located primary binding site, 5'-A-G-C-T-3', flanked on either side by the sequences (AT)(n) or (AA)(n) (with n = 2, 3, 4) and AA(AT)(2), were studied. For different flanking sequences, (AA)(n)-series or (AT)(n)-series, differential fluorescence enhancements of the ligand due to binding were observed. Thermodynamic studies indicated that the flanking sequences not only affected DNA stability and secondary structure but also modulated ligand binding to the primary binding site. The magnitude of the ligand binding affinity to the primary site was inversely related to the sequence dependent stability. The enthalpy of ligand binding was directly measured by isothermal titration calorimetry, and this made it possible to parse the binding free energy into its energetic and entropic terms.

Surface-enhanced resonance Raman spectroscopic study of yeast iso-1-cytochrome c and its mutant

The structural stability and redox properties of yeast iso-1-cytochrome c and its mutant, F82H, were studied by surface-enhanced resonance Raman scattering (SERRS) spectroscopy. Phenylalanine, which exists at the position-82 in yeast iso-1-cytochrome c, is replaced by histidine in the mutant. The SERRS spectra of the proteins on the bare silver electrodes indicate that the mutant possesses a more stable global structure with regard to the adsorption-induced conformational alteration. The redox potential of the mutant negatively shifts by about 400 mV, relative to that of yeast iso-1-cytochrome c. This is ascribed to axial ligand switching and higher solvent accessibility of the heme iron in the mutant during the redox reactions.

Circular dichroism and resonance Raman comparative studies of wild type cytochrome c and F82H mutant

The UV-visible, circular dichroism (CD), and resonance Raman (RR) spectra of the wild type yeast iso-1-cytochrome c (WT) and its mutant F82H in which phenylalanine-82 (Phe-82) is substituted with His are measured and compared for oxidized and reduced forms. The CD spectra in the intrinsic and Soret spectral region, as well as RR spectra in high, middle, and low frequency regions, are discussed. From the analysis of the spectra, it is determined that in the oxidized F82H the two axial ligands to the heme iron are His-18 and His-82 whereas in the reduced form the sixth ligand switches from His-82 to Met-80 providing the coordination geometry similar to that of WT. Based on the spectroscopic data, the conclusion is that the porphyrin macrocycle is less distorted in the oxidized F82H compared to the oxidized WT. Similar distortions are present in the reduced form of the proteins. Frequency shifts of Raman bands, as well as the decrease of the or-helix content in the CD spectra, indicate more open conformation of the protein around the heme. (C) 2000 John Wiley & Sons, Inc.

Investigation of Pr valence and relationship between bond covalency and T-c in Y1-xPrxBa2Cu3O7 (x = 0-1)

The valence of Pr and relationship between bond covalency and T-c in Y1-xPrxBa2Cu3O7 (x = 0-1) have been studied using complex chemical bond theory. The results indicate that the depression of superconductivity in Y1-xPrxBa2Cu3O7 can be reasonably explained by bond covalency difference for the bonds between CuO2 plane and CuO chain. T-c decreases with the decreasing of bond covalency difference and reaches zero when bond covalency difference is zero (or bond covalency in CuO2 exceeds that in CuO chain) at Pr concentration 0.55 and valence +3.30. These are in good agreement with the experiments and meanwhile suggest that the valence of Pr is + 3.30 in Y1-xPrxBa2Cu3O7. The results also indicate that for Pr valence less than +3.15, superconductivity always exists for whatever Pr concentration, whereas for Pr with a valence of +4.0, superconductivity disappears as soon as Pr concentration exceeds 0.19. This supports with the viewpoint that higher valence Pr will contribute more electrons to CuO2 plane, filling the mobile holes responsible for conduction. For PrBa2Cu3O7 with no Ba-site Pr, our calculation suggests that it will be a superconductor if the average valence of Pr is less than +3.15. (C) 1998 Published by Elsevier Science B.V. All rights reserved.

STRUCTURE AND SITE-SYMMETRY INVESTIGATION ON THE HEXAGONAL KCAY(PO4)(2)

A new double phosphate, KCaY(PO4)(2), isostructural with hexagonal LaPO4, is reported. It crystallizes in the hexagonal system with a = 0.6903 nm and c = 0.6331 nm. Its vibrational spectra, IR and Raman spectra showed that the site symmetry of the PO4 anion slightly deviated from D-2 toward C-2.

Cflec-4, a multidomain C-type lectin involved in immune defense of Zhikong scallop Chlamys farreri

C-type lectins are a superfamily of carbohydrate-recognition proteins which play crucial roles in the innate immunity. In this study, a novel multidomain C-type lectin gene from scallop Chlamys farreri (designated as Cflec-4) was cloned by RACE approach based on EST analysis. The full-length cDNA of Cflec-4 was of 2086 bp. The open reading frame was of 1830 bp and encoded a polypeptide of 609 amino acids, including a signal sequence and four dissimilar carbohydrate-recognition domains (CRDs). The deduced amino acid sequence of CflecA shared high similarities to other C-type lectin family members. The phylogenetic analysis revealed the divergence between the three N-terminal CRDs and the C-terminal one, suggesting that the four CRDs in Cflec-4 originated by repeated duplication of different primordial CRD. The potential tertiary structure of each CRD in Cflec-4 was typical double-loop structure with Ca2+-binding site 2 in the long loop region and two conserved disulfide bridges at the bases of the loops. The tissue distribution of Cflec-4 mRNA was examined by fluorescent quantitative real-time PCR. In the healthy scallops, the Cflec-4 transcripts could be only detected in gonad and hepatopancreas, whereas in the Listonella anguillarum challenged scallops, it could be also detected in hemocytes. These results collectively suggested that CflecA was involved in the immune defense of scallop against pathogen infection and provided new insight into the evolution of C-type lectin superfamily. (C) 2009 Elsevier Ltd. All rights reserved.

Isolation, properties and spatial site analysis of gamma subunits of B-phycoerythrin and R-phycoerythrin

Polysiphonia urceolata R-phycoerythrin and Porphyridium cruentum B-phycoerythrin were degraded with proteinaseK, and then the nearly native gamma subunits were isolated from the reaction mixture. The process of degradation of phycoerythrin with proteinaseK showed that the gamma subunit is located in the central cavity of (alpha beta)(6) hexamer of phycoerythrin. Comparative analysis of the spectra of the native phycoerythrin, the phycoerythrin at pH 12 and the isolated gamma subunit showed that the absorption peaks of phycoerythrobilins on alpha or beta subunit are at 535 nm (or 545 nm) and 565 nm, the fluorescence emission maximum at 580 nm; the absorption peak of phycoerythrobilins on the isolated gamma subunit is at 589 nm, the fluorescence emission peak at 620 nm which overlaps the absorption maximum of C-phycocyanin and perhaps contributes to the energy transfer with high efficiency between phycoerythrin and phycocyanin in phycobilisome; the absorption maximum of phycourobilin on the isolated gamma subunit is at 498 nm, which is the same as that in native phycoerythrin, and the fluorescence emission maximum at 575 nm.

Molecular cloning, characterization and expression analysis of a putative C-type lectin (Fclectin) gene in Chinese shrimp Fenneropenaeus chinensis

Lectin is regarded as a potential molecule involved in immune recognition and phagocytosis through opsonization in crustacean. Knowledge on lectin at molecular level would help us to understand its regulation mechanism in crustacean immune system. A novel C-type lectin gene (Fclectin) was cloned from hemocytes of Chinese shrimp Fenneropenaeus chinensis by 3' and 5' rapid amplification of cDNA ends (RACE) PCR. The full-length cDNA consists of 1482 bp with an 861 bp open reading frame, encoding 287 amino acids. The deduced amino acid sequence contains a putative signal peptide of 19 amino acids. It also contains two carbohydrate recognition domains/C-type lectin-like domains (CRD1 and CRD2), which share 78% identity with each other. CRD1 and CRD2 showed 34% and 30% identity with that of mannose-binding lectin from Japanese lamprey (Lethenteron japonicum), respectively. Both CRD1 and CRD2 of Fclectin have I I amino acids residues, which are relatively invariant in animals' C-type lectin CRDs. Five residues at Ca2+ binding site I are conserved in Fclectin. The potential Ca2+/carbohydrate-binding (site 2) motif QPD, E, NP (Gln-Pro-Asp, Glu, Asn-Pro) presented in the two CRDs of Fclectin may support its ability to bind galactose-type sugars. It could be deduced that Fclectin is a member of C-type lectin superfamily. Transcripts of Fclectin were found only in hemocytes by Northern blotting and RNA in situ hybridization. The variation of mRNA transcription level in hemocytes during artificial infection with bacteria and white spot syndrome virus (WSSV) was quantitated by capillary electrophoresis after RT-PCR. An exploration of mRNA expression variation after LPS stimulation was carried out in primarily cultured hemocytes in vitro. Expression profiles of Fclectin gene were greatly modified after bacteria, LPS or WSSV challenge. The above-stated data can provide us clues to understand the probable role of C-type lectin in innate immunity of shrimp and would be helpful to shrimp disease control. (c) 2006 Elsevier Ltd. All rights reserved.