Rho and riboswitch-dependent regulations of mntP gene expression evade manganese and membrane toxicities.

The trace metal ion manganese (Mn) in excess is toxic. Therefore, a small subset of factors tightly maintains its cellular level, among which an efflux protein MntP is the champion. Multiple transcriptional regulators and a manganese-dependent translational riboswitch regulate the MntP expression in Escherichia coli.

Effect of ligand substituents on the reactivity pathways of copper(II) complexes towards electrocatalytic water oxidation.

The electrocatalytic water oxidation activity of three copper(II) complexes [Cu(L1H)(L)](ClO) (1), [Cu(L2H)(L)(HO)](ClO) (2) and [Cu(L3H)(L)](ClO) (3) with aryl oxime ligands L1H, L2H and L3H [L1H = 1-(pyridin-2-yl)methanone oxime, L2H = 1-(pyridin-2-yl)ethanone oxime and L3H = 1-(pyridin-2-yl)propanone oxime] was investigated. All the three ligands have in common a pyridyl group attached to the carbon centre of the oxime moiety and differ in the second substituent attached to the carbon centre. Electrochemical investigation of the catalytic activity of complexes 1, 2 and 3 shows that the nature of the substituent attached to the carbon centre has an influence on the catalytic pathway and overall catalytic activity of these complexes.

Catalytic and Electrochemical Study of Cu-ZSM-5/MCM-41.

Hierarchically structured micro-mesoporous ZSM-5/MCM-41 composite materials incorporating copper ions were synthesized using pre-synthesized ZSM-5 and cetyltrimethylammonium bromide (CTAB) as a template for forming the MCM-41 structure. The composites were characterized through powder X-ray diffraction, N adsorption-desorption, diffuse reflectance spectroscopy (UV-vis DRS), Fourier transform infrared spectroscopy, thermogravimetric analysis, scanning electron microscopy, and energy dispersive X-ray spectroscopy. X-ray diffraction confirmed well-ordered ZSM-5 and MCM-41 structures, and UV-vis DRS showed successful copper ion incorporation.