In this study, simplex centroid mixture design was employed to determine the effect of urea on ZnO-CeO. The heterojunction materials were synthesized using a solid-state combustion method, and the physicochemical properties were evaluated using X-ray diffraction, nitrogen adsorption/desorption, and UV-Vis spectroscopy. Photocatalytic activity was determined by a triclosan degradation reaction under UV irradiation.
View Article and Find Full Text PDFPolypyridyl ruthenium complexes have been intensively investigated for their remarkable antiproliferative properties and some are currently being tested in clinical trials. Here, we investigated the impact of illumination on the biological properties of a series of new cyclometalated ruthenium compounds with increased π-conjugation. We determined that various of these complexes display a bivalent biological activity as they are highly cytotoxic by themselves in absence of light while their cytotoxicity can significantly be elevated towards an IC in the nanomolar range upon illumination.
View Article and Find Full Text PDFLactate dehydrogenase (LDH) is a redox enzyme often overexpressed in cancer cells allowing their survival in stressful metabolic tumor environment. Ruthenium(II) complexes have been shown to impact on the activity of purified horseradish peroxidase and glucose oxidase but the physiological relevance remains unclear. In this study we investigated how ruthenium complexes impact on the activity of LDH in vitro and in cancer cells and performed a comparative study using polypyridine ruthenium(II) complex [Ru(bpy)] (1) and its structurally related cyclometalated 2-phenylpyridinato counterpart [Ru(phpy)(bpy)] (2) (bpy=2,2'-bipyridine, phpyH=2-phenylpyridine).
View Article and Find Full Text PDFCyclometalated Ru(II) derivatives of 2-phenylpyridine (Hphpy) [Ru(phpy)(bpy)2]Cl (1a) and [Ru(phpy)(phen)2]Cl (1b) (bpy is 2,2'-bipyridine, phen is 1,10-phenanthroline) behave as noncompetitive inhibitors of glucose oxidase from Aspergillus niger in the enzyme-catalyzed oxidation of D-glucose by O2 into the corresponding lactone at pH 5.0 and 25 °C. The enzymatic activity has been measured by monitoring the O2 consumption.
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