Synthesis and characterization of two cobalt(II) complexes based on 4,6-bis(2-pyridyl)-1,3,5-triazin-2-ol

<p>Two cobalt(II) complexes based on 4,6-bis(2-pyridyl)-1,3,5-triazin-2-ol (HOBPT), [Co₃(OBPT)(<i>μ</i>³−OH)(SO₄)₂(H₂O)₃]·2H₂O (<b>1</b>) and [Co(OBPT)₂]·2H₂O (<b>2</b>) were obtained. Single-crystal X-ray diffraction analyses indicate that <b>1</b> is a two-dimensional (2D) structure and the ligand adopts mono/bis-bidentate coordination; this coordination mode of this ligand was never found before. Magnetic properties of <b>1</b> have been studied, showing that <b>1</b> is a spin canted belt. Much different from <b>1</b>, <b>2</b> is a discrete structure with tridentate ligand with its hydroxyl group deprotonated but uncoordinated. Lattice water molecules in <b>2</b> link to four-membered water clusters, which linked the [Co(OBPT)₂] to 1-D chains along the <i>b</i> axis.</p

DataSheet1.zip

<p>NAD(H) and NADP(H) are essential co-enzymes which dominantly control a number of fundamental biological processes by acting as reducing power and maintaining the intracellular redox balance of all life kingdoms. As the only enzymes that catalyze NAD(H) and ATP to synthesize NADP(H), NAD Kinases (NADKs) participate in many essential metabolic reactions, redox sensitive regulation, photosynthetic performance and also reactive oxygen species (ROS) homeostasis of cells and therefore, play crucial roles in both development and stress responses of plants. NADKs are highly conserved enzymes in amino acid sequences but have multiple subcellular localization and diverse functions. They may function as monomers, dimers or multimers in cells but the enzymatic properties in plants are not well elucidated yet. The activity of plant NADK is regulated by calcium/calmodulin and plays crucial roles in photosynthesis and redox co-enzyme control. NADK genes are expressed in almost all tissues and developmental stages of plants with specificity for different members. Their transcripts can be greatly stimulated by a number of environmental factors such as pathogenic attack, irritant applications and abiotic stress treatments. Using transgenic approaches, several studies have shown that NADKs are involved in chlorophyll synthesis, photosynthetic efficiency, oxidative stress protection, hormone metabolism and signaling regulation, and therefore contribute to the growth regulation and stress tolerance of plants. In this review, the enzymatic properties and functional mechanisms of plant NADKs are thoroughly investigated based on literature and databases. The results obtained here are greatly advantageous for further exploration of NADK function in plants.</p

Incomplete Spin Crossover versus Antiferromagnetic Behavior Exhibited in Three-Dimensional Porous Fe(II)-Bis(tetrazolate) Frameworks

Two three-dimensional (3D) Fe­(II) porous metal–organic frameworks (MOFs) [Fe₂(H_0.67bdt)₃]·13H₂O (<b>1</b>·13H₂O) and [Fe₃(ox)­(H_0.67bdt)₃(H₂O)₂]·solvent (<b>2</b>·solvent) (H₂bdt = 5,5′-(1,4-phenylene)­bis­(1H-tetrazole); H₂ox = oxalic acid; solvent = 10H₂O and 9CH₃OH for <b>2</b>·9MeOH and 6H₂O and 5C₄H₉OH for <b>2</b>·5<i>n</i>-BuOH) were solvothermally synthesized and characterized. The X-ray structure analysis reveals that complex <b>1</b>·13H₂O is constructed from one-dimensional (1D) {Fe­(tz)₃}_<i>n</i> (tz = tetrazolate) chains which are linked through the phenyl tethers of the bdt ligands into a 3D microporous framework. In the case of complex <b>2</b>·solvent, the linear trinuclear [Fe₃(tz)₆] units are linked by ox^2– bridges to form 1D {Fe₃(tz)₆(ox)}_<i>n</i> chains, which are also extended into a 3D microporous framework linked by the bdt ligands. Their frameworks can be simplified as the same topological network (4⁶,6⁶,8³)­(4²,6³,8). The substructure of the 1D {Fe­(tz)₃}_<i>n</i> chain in <b>1</b>·13H₂O consists of spin-crossover (SCO) active Fe1 ions and low spin (LS) Fe2 ions alternately, while the trinuclear unit in <b>2</b>·solvent contains a partial high spin (HS) Fe1 ion and two terminal HS Fe2 ions. Magnetic susceptibility measurements reveal that complex <b>1</b>·13H₂O presents an incomplete gradual SCO behavior. Although complex <b>2</b>·solvent also has the SCO active Fe1 ions, the spin state change is extremely small and the antiferromagnetic property is primarily observed

Incomplete Spin Crossover versus Antiferromagnetic Behavior Exhibited in Three-Dimensional Porous Fe(II)-Bis(tetrazolate) Frameworks

Two three-dimensional (3D) Fe­(II) porous metal–organic frameworks (MOFs) [Fe₂(H_0.67bdt)₃]·13H₂O (<b>1</b>·13H₂O) and [Fe₃(ox)­(H_0.67bdt)₃(H₂O)₂]·solvent (<b>2</b>·solvent) (H₂bdt = 5,5′-(1,4-phenylene)­bis­(1H-tetrazole); H₂ox = oxalic acid; solvent = 10H₂O and 9CH₃OH for <b>2</b>·9MeOH and 6H₂O and 5C₄H₉OH for <b>2</b>·5<i>n</i>-BuOH) were solvothermally synthesized and characterized. The X-ray structure analysis reveals that complex <b>1</b>·13H₂O is constructed from one-dimensional (1D) {Fe­(tz)₃}_<i>n</i> (tz = tetrazolate) chains which are linked through the phenyl tethers of the bdt ligands into a 3D microporous framework. In the case of complex <b>2</b>·solvent, the linear trinuclear [Fe₃(tz)₆] units are linked by ox^2– bridges to form 1D {Fe₃(tz)₆(ox)}_<i>n</i> chains, which are also extended into a 3D microporous framework linked by the bdt ligands. Their frameworks can be simplified as the same topological network (4⁶,6⁶,8³)­(4²,6³,8). The substructure of the 1D {Fe­(tz)₃}_<i>n</i> chain in <b>1</b>·13H₂O consists of spin-crossover (SCO) active Fe1 ions and low spin (LS) Fe2 ions alternately, while the trinuclear unit in <b>2</b>·solvent contains a partial high spin (HS) Fe1 ion and two terminal HS Fe2 ions. Magnetic susceptibility measurements reveal that complex <b>1</b>·13H₂O presents an incomplete gradual SCO behavior. Although complex <b>2</b>·solvent also has the SCO active Fe1 ions, the spin state change is extremely small and the antiferromagnetic property is primarily observed

Presentation_1_Genome-Wide Identification and Functional Analysis of NADPH Oxidase Family Genes in Wheat During Development and Environmental Stress Responses.pdf

<p>As the key producers of reactive oxygen species (ROS), NADPH oxidases (NOXs), also known as respiratory burst oxidase homologs (RBOHs), play crucial roles in various biological processes in plants with considerable evolutionary selection and functional diversity in the entire terrestrial plant kingdom. However, only limited resources are available on the phylogenesis and functions of this gene family in wheat. Here, a total of 46 NOX family genes were identified in the wheat genome, and these NOXs could be classified into three subgroups: typical TaNOXs, TaNOX-likes, and ferric reduction oxidases (TaFROs). Phylogenetic analysis indicated that the typical TaNOXs might originate from TaFROs during evolution, and the TaFROs located on Chr 2 might be the most ancient forms of TaNOXs. TaNOXs are highly expressed in wheat with distinct tissue or organ-specificity and stress-inducible diversity. A large-scale expression and/or coexpression analysis demonstrated that TaNOXs can be divided into four functional groups with different expression patterns under a broad range of environmental stresses. Different TaNOXs are coexpressed with different sets of other genes, which widely participate in several important intracellular processes such as cell wall biosynthesis, defence response, and signal transduction, suggesting their vital but diversity of roles in plant growth regulation and stress responses of wheat.</p

Haplotype analysis.

<p>Four microsatellite markers (D10S197, D10S196, D10S1652 and D10S537) from 9 related members (II-5, II-6, III-10, III-11, III-12, III-13, III-15, IV-10 and IV-11) demonstrated that the p.C634Y/V292M/R67H/R982C mutation did not arise on a common chromosome; p.C634Y was of maternal origin and p.V292M/R67H/R982C was paternal and located in a common allele.</p

Summary of reported <i>RET</i> double mutations associated with MEN 2.

<p>Summary of reported <i>RET</i> double mutations associated with MEN 2.</p

Clinical presentations of patients with MTC and <i>RET</i> mutations.

<p>*proband; F, female; M, male; Pat, paternal family; Mat, maternal family; Pre-op Ct, pre-operative calcitonin (ng/L); US, ultrasound; AS, awaiting surgery; ADM, age at diagnosis of MTC; pTNM, tumour stage; TT, total thyroidectomy; Bi-, Bilateral; No spec, no specimen.</p>a<p>LN+ includes positive lymph nodes proven on histopathology; resected includes lymph node resected.</p

Portion of genomic DNA and RT-PCR product sequencing from tumor tissues.

<p>A, Direct sequencing consequences of RT-PCR products from PHEO tissue of III-12 indicated a heterozygous G/A mutation at codon 634, which was consistent with the results of DNA from blood and tumor tissues and whole exome sequencing. B, C, D, Direct sequencing consequences of RT-PCR products from MTC tissue of III-11 indicated heterozygous G/A, C/T, and G/A mutations at codons 292, 982, and 67, respectively, which was consistent with the results of DNA from blood and tumor tissues and whole exome sequencing.</p

Portion of DNA sequences and polyacrylamide gel electrophoresis analysis of restriction endonuclease digestion.

<p>A, Maternal origin MEN 2A (III-23, III-12 and IV-10) were heterozygous for c.G2901A (p.C634Y), whereas paternal origin members (III-11, III-6, II-5, II-6 and III-3) were homozygous for the wild-type allele. This mutation was confirmed by <i>Kpn</i> I digestion. B, IV-10 and paternal origin FMTC (III-11, II-5, and III-3) demonstrated a heterozygous c.G874A (p.V292M) mutation which created the restriction enzyme site for <i>Nco</i> I, whereas maternal origin members (III-12 and IV-11), and two unaffected paternal members (III-10 and IV-8) showed the normal sequence. C, A heterozygous c.C2944T (p.R982C) polymorphism from IV-10 and paternal origin FMTC (III-11, II-5 and III-3) was found, whereas the maternal origin members III-12 and IV-11 and two unaffected paternal members (III-10 and IV-8) were homozygous for the wild-type allele. This polymorphism was validated by <i>Rsa</i> I digestion.</p