Photocurrent and Gelation Properties of Polyphenol-Modified Titanium-Oxo Compounds.

Organic-inorganic hybrid metal-polyphenols as stable structural modules have gained extensive interest due to their diverse applications. However, titanium-oxo compounds (TOCs) with large molecular polyphenols have been less explored, and they were expected to be different from small polyphenols with isolated metal ions. Herein, 4-methyl-esculetin (Mesc), a catechol derivative, was selected to construct three TOCs, namely, [Ti17O24(Mesc)4(OiPr)16] (1), [Ti12O14(OiPr)18][Ti16O14(Mesc)12(OiPr)14] (2), and [Ti3O(Mesc)2(OAc)2(OiPr)4] (3). These compounds were structurally characterized. Photocurrent responses were evaluated using the compound-sensitized TiO2 electrodes. It was found that the current densities of 1-3 electrodes are in the order of 1 ≫ 3 > 2, which relates to the ligand-to-TiO core and ligand-to-ligand charge transfers (LMCT and LLCT, respectively). Density functional theory calculations showed that the lowest band gap of 1 originates from its LLCT. Compound 1 reacted with polyphenol tannin (TA) to form a fully transparent and robust gel (1-TA), and the gelation properties were investigated. Using the gel as a nano-TiO2 fixing agent, solar cell electrodes were prepared by a low-temperature wet method. The photocurrent responsive behavior of the 1-TA/TiO2 electrode was compared with that of the 1-sensitized traditional high-temperature-treated TiO2 electrode. Although the current density of the former is somewhat lower than that of the traditional electrode, the low-temperature wet preparation of the 1-TA/TiO2 electrode is more energy-efficient and sustainable.

2D Lead Iodide Perovskite with Mercaptan-Containing Amine and Its Exceptional Water Stability.

Two dimensional (2D) hybrid perovskites have attracted a great deal of interest because of their appropriate photovoltaic efficiency and environmental stability. Although some 2D hybrid perovskites with sulfur-containing amines have been reported, the cation having the mercaptan group has not been well explored yet. In this work, cysteamine (Cya, HS(CH2)2NH2), a mercaptan-containing amine, was introduced into 2D hybrid perovskite. Two 2D lead iodides with different structures, (HCya)2PbI4 (1) and (HCya)7Pb4I15 (2), were isolated as a red low-temperature phase and a yellow high-temperature phase, respectively. X-ray single-crystal structural analysis showed that the red phase 1 is a single layered corner-shared perovskite and that the yellow phase 2 is a corner/edge-shared quasi-2D perovskite. A thermo-induced reversible 1 to 2 phase transition was found in this synthetic system. The configuration of HCya cation greatly influences the crystallization equilibrium, generating different structures of the lead halides. The single-crystal structure of 1 is discussed in comparison with that of (HAE)2PbI4 (AE = HO(CH2)2NH2), an analogue of 1. The different effects of OH and SH groups on the 2D frameworks are studied based on their hydrogen bonding properties. More remarkably, although the two perovskites have similar structures, the (HCya)2PbI4 (1) has an intrinsic water stability that is much more stable than (HAE)2PbI4, which should be attributed to the affinity of the SH group with lead on the surface of the lead halide.

Structural insights into immunoglobulin M.

Immunoglobulin M (IgM) plays a pivotal role in both humoral and mucosal immunity. Its assembly and transport depend on the joining chain (J-chain) and the polymeric immunoglobulin receptor (pIgR), but the underlying molecular mechanisms of these processes are unclear. We report a cryo-electron microscopy structure of the Fc region of human IgM in complex with the J-chain and pIgR ectodomain. The IgM-Fc pentamer is formed asymmetrically, resembling a hexagon with a missing triangle. The tailpieces of IgM-Fc pack into an amyloid-like structure to stabilize the pentamer. The J-chain caps the tailpiece assembly and bridges the interaction between IgM-Fc and the polymeric immunoglobulin receptor, which undergoes a large conformational change to engage the IgM-J complex. These results provide a structural basis for the function of IgM.

Advanced Nanoclay-Based Nanocomposite Solid Polymer Electrolyte for Lithium Iron Phosphate Batteries.

High-performance solid polymer electrolytes (SPEs) have long been desired for the next generation of lithium batteries. One of the most promising ways to improve the morphological and electrochemical properties of SPEs is the addition of fillers with specific nanostructures. However, the production of such fillers is generally expensive and requires complicated preparation procedures. Halloysite nanotubes (HNTs), with their tubular structure, resemble carbon nanotubes in terms of geometric features and can be obtained at a relatively low cost. Previously, we reported that the HNT poly(ethylene oxide) composite SPE possesses excellent electrochemical and mechanical properties and outstanding cycling performance for all-solid-state lithium sulfur batteries. However, the HNT/SPE was not effective for lithium iron phosphate (LFP) batteries. The compatibility between the electrodes and the electrolyte sharply decreased, and no decent cycling performance was achieved. Therefore, a modification was studied which involves a minor addition of LFP during the preparation procedure. With this modification, good ionic conductivity (9.23 × 10-5 S cm-1 at 25 °C) is achieved, and compatibility between the electrodes and the electrolyte is enhanced. At the same time, an electrochemical stability window of 5.14 V and lithium-ion transference number of 0.46 are found. All-solid-state LFP batteries possessing excellent cycling performance are further demonstrated.

Secretory kinase Fam20C tunes endoplasmic reticulum redox state via phosphorylation of Ero1α.

Family with sequence similarity 20C (Fam20C), the physiological Golgi casein kinase, phosphorylates numerous secreted proteins that are involved in a wide variety of biological processes. However, the role of Fam20C in regulating proteins in the endoplasmic reticulum (ER) lumen is largely unknown. Here, we report that Fam20C interacts with various luminal proteins and that its depletion results in a more reduced ER lumen. We further show that ER oxidoreductin 1α (Ero1α), the pivotal sulfhydryl oxidase that catalyzes disulfide formation in the ER, is phosphorylated by Fam20C in the Golgi apparatus and retrograde-transported to the ER mediated by ERp44. The phosphorylation of Ser145 greatly enhances Ero1α oxidase activity and is critical for maintaining ER redox homeostasis and promoting oxidative protein folding. Notably, phosphorylation of Ero1α is induced under hypoxia, reductive stress, and secretion-demanding conditions such as mammalian lactation. Collectively, our findings open a door to uncover how oxidative protein folding is regulated by phosphorylation in the secretory pathway.

Ag-K/MnO2 nanorods as highly efficient catalysts for formaldehyde oxidation at low temperature.

A series of Ag-K/MnO2 nanorods with various molar ratios of K/Ag were synthesized by a conventional wetness incipient impregnation method. The as-prepared catalysts were used for the catalytic oxidation of HCHO. The Ag-K/MnO2 nanorods with an optimal K/Ag molar ratio of 0.9 demonstrated excellent HCHO conversion efficiency of 100% at a low temperature of 60 °C. The structures of the samples were investigated by BET, TEM, SEM, XRD, H2-TPR, O2-TPD and XPS. The results showed that Ag-0.9K/MnO2-r exhibited more facile reducibility and greatly abundant surface active oxygen species, endowing it with the best catalytic activity of the studied catalysts. This work provides new insights into the development of low-cost and highly efficient catalysts for the removal of HCHO.

Structure of Fam20A reveals a pseudokinase featuring a unique disulfide pattern and inverted ATP-binding.

Mutations in FAM20A cause tooth enamel defects known as Amelogenesis Imperfecta (AI) and renal calcification. We previously showed that Fam20A is a secretory pathway pseudokinase and allosterically activates the physiological casein kinase Fam20C to phosphorylate secreted proteins important for biomineralization (Cui et al., 2015). Here we report the nucleotide-free and ATP-bound structures of Fam20A. Fam20A exhibits a distinct disulfide bond pattern mediated by a unique insertion region. Loss of this insertion due to abnormal mRNA splicing interferes with the structure and function of Fam20A, resulting in AI. Fam20A binds ATP in the absence of divalent cations, and strikingly, ATP is bound in an inverted orientation compared to other kinases. Fam20A forms a dimer in the crystal, and residues in the dimer interface are critical for Fam20C activation. Together, these results provide structural insights into the function of Fam20A and shed light on the mechanism by which Fam20A mutations cause disease.

Structure of protein O-mannose kinase reveals a unique active site architecture.

The 'pseudokinase' SgK196 is a protein O-mannose kinase (POMK) that catalyzes an essential phosphorylation step during biosynthesis of the laminin-binding glycan on α-dystroglycan. However, the catalytic mechanism underlying this activity remains elusive. Here we present the crystal structure of Danio rerio POMK in complex with Mg2+ ions, ADP, aluminum fluoride, and the GalNAc-ß3-GlcNAc-ß4-Man trisaccharide substrate, thereby providing a snapshot of the catalytic transition state of this unusual kinase. The active site of POMK is established by residues located in non-canonical positions and is stabilized by a disulfide bridge. GalNAc-ß3-GlcNAc-ß4-Man is recognized by a surface groove, and the GalNAc-ß3-GlcNAc moiety mediates the majority of interactions with POMK. Expression of various POMK mutants in POMK knockout cells further validated the functional requirements of critical residues. Our results provide important insights into the ability of POMK to function specifically as a glycan kinase, and highlight the structural diversity of the human kinome.

Metal centered oxidation or ligand centered oxidation of metal dithiolene? Spectral, electrochemical and structural studies on a nickel-4-pyridine-1,2-dithiolate system.

The complex Et(4)N[Ni(4-pedt)(2)] (1) (4-pedt = 1-(pyridine-4-yl) ethylene-1,2-dithiolate) was synthesized to investigate the behaviour of metal dithiolene compounds upon protonation and oxidation by absorption spectroscopy, electrochemistry and structural analyses and to further understand the electronic states of the dithiolene compounds. It is unexpected that the 915 nm NIR transition band is not shifted when H(+) is added, and it is only affected (blue-shifted) when the compound is oxidized. All the evidence of electronic spectra indicates that the NIR band is relevant to the central [Ni(edt)(2)] moiety (edt = ethylenedithiolate), not the behaviour of individual Ni ions or ligands. It is also not the band of intermolecular interaction of a dimer. The moderately intense band appearing at 655 nm upon protonation is assigned to the intramolecular charge-transfer band between the [Ni(edt)(2)] moiety and the pyridine. The redox potentials of the metal dithiolene are sensitive to the protonation of the pyridyl group. The structures of monocationic complex and the protonated compounds [Ni(4-Hpedt)(2)]·ClO(4)·H(2)O (2) and [Ni(4-Hpedt)(2)]·PhSO(3)·2DMF (3) were characterized by single crystal X-ray determination. The structural data demonstrate that the oxidation of the monoanionic dithiolene complex to neutral does not change the Ni-S bond distances obviously, which further indicates that the process is not only the metal centered oxidation.

3-D germanate constructed with Ge7 cluster layers and nickel-ethanolamine linkage.

A Ge(7) germanate, [Ni(H(2)O)(µ-C(2)H(6)NO)(2)Ge(7)O(14)(C(2)H(7)NO)]·C(2)H(5)OH (1), was prepared by the solvothermal method using ethanolamine (C(2)H(7)NO) as solvent, ligand, and structure-directing agent. Compound 1 shows an unusual GeO framework fused with transition metal complex. The 2-D layers of Ge(7) clusters are linked by a [Ni(H(2)O)(µ-C(2)H(6)NO)(2)] moiety, forming a 3-D architecture. The preparation and structure of 1 are discussed in comparison with the Ge(9) germanates decorated with metal ethylenediamine complexes. The hydroxyl group of the ethanolamine plays an important role in formation of the 3-D structure, in which the ligand ethanolamine is coordinated directly onto the Ge cluster by the hydroxyl group. It is a new type of germanates incorporated with a TM complex bridge. The proton on the flexible amine side can be exchanged by alkali metal ions.