Beringstafford2803

A portable paper-based organic redox flow primary battery using sustainable quinone chemistry is presented. The compact prototype relies on the capillary forces of the paper matrix to develop a quasi-steady flow of the reactants through a pair of porous carbon electrodes without the need of external pumps. Co-laminar capillary flow allows operation Under mixed-media conditions, in which an alkaline anolyte and an acidic catholyte are employed. This feature enables higher electrochemical cell voltages during discharge operation and the utilization of a wider range of available species and electrolytes and provides the advantage to form a neutral or near-neutral pH as the electrolytes neutralize at the absorbent pad, which allows a safe disposal after use. The effects of the device design parameters have been studied to enhance battery features such as power output, operational time, and fuel utilization. The device achieves a faradaic efficiency of up to 98 %, which is the highest reported in a capillary-based electrochemical power source, as well as a cell capacity of up to 11.4 Ah L-1  cm-2 , comparable to state-of-the-art large-scale redox flow cells. © 2020 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.Vip3A proteins are widely used for controlling pest Lepidoptera. Different binding sites with different receptors in the insect midgut membrane and lack of cross-resistance with crystal (Cry) proteins enhance their applicability, as both single proteins and proteins pyramided with Cry proteins in transgenic Bt crops. Vip3A proteins are effective but there is relatively little information about their structure, function, activation, specificity, and mode of action. In addition, the mechanism of insect resistance to these proteins is unknown. Phylogenetic analysis and multiple sequence alignment showed that Vip3A proteins are genetically distant from Cry proteins. The mode of action and insecticidal activity of Vip3A proteins are discussed in this review. This review also provides detailed information about the Vip3A protein family that may aid in the design of more efficient pest management strategies in response to insect resistance to insecticidal proteins. © 2020 Society of Chemical Industry.Several H-H bond forming pathways have been proposed for the hydrogen evolution reaction (HER). Revealing these HER mechanisms is of fundamental importance for the rational design of catalysts and is also extremely challenging. Herein we report an unparalleled example of switching between homolytic and heterolytic HER mechanisms. We designed and synthesized three nickel(II) porphyrins with distinct steric effects by introducing bulky amido moieties to ortho- or para-positions of the meso-phenyl groups. We furthermore showed their different catalytic HER behaviors. For these Ni porphyrins, although their 1e-reduced forms are active to reduce trifluoroacetic acid, the resulted Ni hydrides - depending on the steric effects of porphyrin rings - have different pathways to make H2. Understanding HER processes, especially controllable switching between homolytic and heterolytic H-H bond formation pathways through molecular engineering, is unprecedented in fundamentals of electrocatalysis. © 2020 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.RNA polymerase II (RNAPII) transcription is crucial for gene expression. RNAPII density peaks at gene boundaries, associating these key regions for gene expression control with limited RNAPII movement. The connections between RNAPII transcription speed and gene regulation in multicellular organisms are poorly understood. Here, we directly modulate RNAPII transcription speed by point mutations in the second largest subunit of RNAPII in Arabidopsis thaliana. Tulmimetostat 2 inhibitor A RNAPII mutation predicted to decelerate transcription is inviable, while accelerating RNAPII transcription confers phenotypes resembling auto-immunity. Nascent transcription profiling revealed that RNAPII complexes with accelerated transcription clear stalling sites at both gene ends, resulting in read-through transcription. The accelerated transcription mutant NRPB2-Y732F exhibits increased association with 5' splice site (5'SS) intermediates and enhanced splicing efficiency. Our findings highlight potential advantages of RNAPII stalling through local reduction in transcription speed to optimize gene expression for the development of multicellular organisms. © 2020 The Authors. Published under the terms of the CC BY NC ND 4.0 license.Conformations of disulfide and diselenide were compared in (Boc-Cys/Sec-NHMe)2 and (Boc-Cys/Sec-OMe)2 using X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, density functional theory (DFT), and circular dichroism (CD) spectroscopy. Conformations of disulfide/diselenide in polypeptides are defined based on the sign of side chain torsion angle χ3 (-CH2 -S/Se-S/Se-CH2 -); negative indicates left-handed and positive indicates right-handed orientation. In the crystals of (Boc-Cys-OMe)2 and (Boc-Sec-OMe)2 , the disulfide exhibits a left-handed and the diselenide a right-handed orientation. Characterization of cystine and selenocystine derivatives in solution using 1 H-NMR, natural abundant 77 Se NMR, 2D-ROESY, and chemical shift analysis coupled to DMSO titration has indicated the symmetrical nature and antiparallel orientation of Cys/Sec residues about the disulfide/diselenide bridges. Structural calculations of cystine and selenocystine derivatives using DFT further support the antiparallel orientation of Cys/Sec residues about disulfide/diselenide. The far-ultraviolet (UV) region CD spectra of cystine and selenocystine derivatives have exhibited the negative Cotton effect (CE) for disulfide and positive for diselenide confirming the difference in the conformational preference of disulfide and diselenide. In the previously reported polymorphic structure of (Boc-Sec-OMe)2 , the diselenide has right-handed orientation. In the X-ray structures of disulfide and diselenide analogues of Escherichia coli protein encoded by curli specific gene C (CgsC) retrieved from Protein Databank (PDB), disulfide has left-handed and the diselenide right-handed orientation. The current report provides the evidence for the local conformational difference between a disulfide and a diselenide group under unconstrained conditions, which may be useful for the rational replacement of disulfide by diselenide in polypeptide chains. © 2020 European Peptide Society and John Wiley & Sons, Ltd.