UV and pulsed electron beam radiation for effective bisphenol A degradation.

The paper presents the results of studying the efficiency of the bisphenol A transformation in water exposed to ultraviolet radiation and a high-energy-pulse-electron beam (e-beam). It has been shown that in both cases, degradation of dissolved bisphenol A occurs, accompanied by an increase in the absorption coefficient in the wavelength region of more than 300 nm. After exposure, products were recorded that fluoresced in the region of more than λ = 400 nm. The fluorescent transformation product of bisphenol A in water (λ = 425 nm) was maximum formatted after an KrCl excilamp irradiated, and under the action of an e-beam, the accumulation of this product was minimal. Under e-beam radiation (170 keV) the efficiency of bisphenol A (1 mM) removal reached 97%. The data obtained allow us to develop ideas about photolysis and radiolysis in natural water systems when knowledge about targeted and optimal conditions for the degradation of bisphenol A is needed.

The Conversion and Degradation of Sulphaguanidine under UV and Electron Beam Irradiation Using Fluorescence.

The work presents a spectral-luminescent study of the sulfaguanidine transformation in water under a pulsed e-beam and UV irradiation of an UVb-04 bactericidal mercury lamp (from 180 to 275 nm), KrCl (222 nm), XeBr (282 nm) and XeCl (308 nm) excilamps. Fluorescent decay curves have been used in our analysis of the sulfaguanidine decomposition. The conversion of antibiotic under e-beam irradiation for up to 1 min was more than 80%, compared with UV radiation: UVb-04-26%, XeBr - 20%. KrCl and XeCl - about 10%. At the end of 64 min of irradiation with UVb-04 and XeBr lamps, the conversion was 99%. During irradiation with these lamps, sulfaguanidine almost completely decomposed and passed into the final fluorescent photoproducts. After e-beam irradiated at the end of 13 min the decrease in sulfaguanidine was 93%. At the same time, the formation of sulfaguanidine transformation products was minimal compared to UV irradiation. The effect of UV irradiation and a powerful e-beam on the decomposition mechanisms of sulfaguanidine are significantly different, which is manifested in various changes in the absorption and fluorescence spectra.

Structure and Vibrational Spectroscopy of C82 Fullerenol Valent Isomers: An Experimental and Theoretical Joint Study.

Gd@C82OxHy endohedral complexes for advanced biomedical applications (computer tomography, cancer treatment, etc.) were synthesized using high-frequency arc plasma discharge through a mixture of graphite and Gd2O3 oxide. The Gd@C82 endohedral complex was isolated by high-efficiency liquid chromatography and consequently oxidized with the formation of a family of Gd endohedral fullerenols with gross formula Gd@C82O8(OH)20. Fourier-transformed infrared (FTIR) spectroscopy was used to study the structure and spectroscopic properties of the complexes in combination with the DFTB3 electronic structure calculations and infrared spectra simulations. It was shown that the main IR spectral features are formed by a fullerenole C82 cage that allows one to consider the force constants at the DFTB3 level of theory without consideration of gadolinium endohedral ions inside the carbon cage. Based on the comparison of experimental FTIR and theoretical DFTB3 IR spectra, it was found that oxidation of the C82 cage causes the formation of Gd@C82O28H20, with a breakdown of the integrity of the parent C82 cage with the formation of pores between neighboring carbonyl and carboxyl groups. The Gd@C82O6(OOH)2(OH)18 endohedral complex with epoxy, carbonyl and carboxyl groups was considered the most reliable fullerenole structural model.

Unusual shift in the visible absorption spectrum of an active ctenophore photoprotein elucidated by time-dependent density functional theory.

Active hydromedusan and ctenophore Ca2+-regulated photoproteins form complexes consisting of apoprotein and strongly non-covalently bound 2-hydroperoxycoelenterazine (an oxygenated intermediate of coelenterazine). Whereas the absorption maximum of hydromedusan photoproteins is at 460-470 nm, ctenophore photoproteins absorb at 437 nm. Finding out a physical reason for this blue shift is the main objective of this work, and, to achieve it, the whole structure of the protein-substrate complex was optimized using a linear scaling quantum-mechanical method. Electronic excitations pertinent to the spectra of the 2-hydroperoxy adduct of coelenterazine were simulated with time-dependent density functional theory. The dihedral angle of 60° of the 6-(p-hydroxy)-phenyl group relative to the imidazopyrazinone core of 2-hydroperoxycoelenterazine molecule was found to be the key factor determining the absorption of ctenophore photoproteins at 437 nm. The residues relevant to binding of the substrate and its adopting the particular rotation were also identified.