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1.
J Colloid Interface Sci ; 578: 326-337, 2020 Oct 15.
Article in English | MEDLINE | ID: mdl-32531562

ABSTRACT

Bismuth oxybromide (BiOBr) nanosheet arrays (NSAs) were successfully prepared on the surface of indium tin oxide glass (hydrophilic pretreated) by solvothermal method using [C16mim]Br ionic liquid as bromine source and template. The effects of different reaction temperatures on array synthesis were investigated. BiOBr NSA-160 (NSAs prepared at 160 °C for 8 h) had the best photoelectrocatalytic (PEC) activity. The removal rate of ciprofloxacin hydrochloride by BiOBr NSA-160 was 91.4% by applying a bias voltage of 0.9 V and irradiating under visible light for 180 min. Results of the analyses of the morphology, photoelectric properties, energy band structure, and degradation active species show that BiOBr NSA-160 is a p-type photocatalyst with a thickness of approximately 500 nm, a light response range of less than 440 nm, and photocurrent density of 69 µA/cm2 at the optimal bias voltage is 0.9 V. The high PEC activity of BiOBr NSA-160 was deduced from two aspects: one is that the bias potential effectively improves the separation efficiency of photogenerated carrier, and the other is that the structure of the nanoarray increases light absorption and active sites. BiOBr NSAs are promising PEC material for application in pollutant removal.

2.
Spectrochim Acta A Mol Biomol Spectrosc ; 118: 765-75, 2014 Jan 24.
Article in English | MEDLINE | ID: mdl-24144830

ABSTRACT

The absorption spectra of Cu(2+), Pb(2+), Cd(2+), and Ni(2+) chelates of an amphoteric chelating polymer flocculant (ACPF) were measured by ultraviolet spectrophotometry, and their compositions and stability constants (ß) were calculated. ACPF exhibited three apparent absorption peaks at 204, 251, and 285 nm. The CSS(-) group of ACPF reacted with Cu(2+), Ni(2+), Pb(2+), and Cd(2+) to form ACPF-Cu(2+), ACPF-Ni(2+), ACPF-Pb(2+), and ACPF-Cd(2+) chelates, respectively, according to a molar ratio of 2:1. The maximum absorption peaks of ACPF-Cu(2+), ACPF-Ni(2+), ACPF-Pb(2+), and ACPF-Cd(2+) appeared at 319, 326, 310, and 313.5 nm, respectively. The maximum absorption peaks of the chelates showed significant red shifting compared with the absorption peaks of ACPF. The ß values of the ACPF-Cu(2+), ACPF-Pb(2+), ACPF-Cd(2+), and ACPF-Ni(2+) chelates were (1.37±0.35)×10(12), (3.26±0.39)×10(11), (2.05±0.27)×10(11), and (3.04±0.45)×10(10), respectively. The leaching rate of heavy metal ions from the chelating precipitates decreased with increasing pH. ACPF-Cu(2+), ACPF-Ni(2+), ACPF-Pb(2+), and ACPF-Cd(2+) were very stable at pH≥5.6. Cu(2+), Ni(2+), Pb(2+), and Cd(2+) concentrations in the leaching liquors were lower than the corresponding limits specified by the Integrated Wastewater Discharge Standard of China.


Subject(s)
Cadmium/chemistry , Chelating Agents/chemistry , Copper/chemistry , Lead/chemistry , Nickel/chemistry , Polymers/chemistry , Flocculation , Hydrogen-Ion Concentration , Spectrophotometry, Ultraviolet
3.
Article in English | MEDLINE | ID: mdl-22503872

ABSTRACT

Spiro pyrrolidines, which were proved with diverse and potent biological activities and they were discovered widespread in nature. In this paper, using fluorescence and ultraviolet spectroscopy, we investigated the interactions between novel spiro pyrrolidine (NSP) and bovine serum albumin (BSA) under the imitated physiological condition. The results show that the NSP binds to BSA molecules. Static quenching and non-radiation energy transfer are the main reasons for fluorescence quenching. We calculated the binding constant (K(a)) and binding sites (n) at different temperatures and obtained the binding distance between the tryptophan residue in BSA and the NSP based on the Förster theory of non-radiation energy transfer. In addition, using synchronous fluorescence spectra, we demonstrated conformation changes of BSA caused by NSP. The comparison of binding potency of NSP and BSA suggests that the substituent on the benzene ring influences the binding ability of NSP and BSA.


Subject(s)
Pyrrolidines/metabolism , Serum Albumin, Bovine/metabolism , Spiro Compounds/metabolism , Animals , Binding Sites , Cattle , Energy Transfer , Kinetics , Molecular Conformation , Protein Binding , Pyrrolidines/chemistry , Serum Albumin, Bovine/chemistry , Spectrometry, Fluorescence , Spectrophotometry, Ultraviolet , Spiro Compounds/chemistry , Temperature
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