Carbon nanotubes as electronic mediators combined with Bi2MoO6and g-C3N4to form Z-scheme heterojunctions to enhance visible light photocatalysis.

In this paper, Z-scheme Bi2MoO6/CNTs/g-C3N4composite photocatalysts were prepared through a simple hydrothermal method. The analysis was performed by XRD, FT-IR, SEM, EDS, TEM, HRTEM, XPS, BET, UV-Vis diffuse reflectance and PL spectrums. Various analyses show that CNTs not only act as excellent charge transfer bridges, but also enable a formation of the Z-scheme of charge transfer mechanism between Bi2MoO6and g-C3N4. This process not only effectively isolates electrons and holes, but also prolongs electron-hole pair lifetimes, resulting in a substantial improvement in the photocatalytic performance of the composite photocatalyst. Best photocatalytic degradation performance was shown by Bi2MoO6/CNTs/g-C3N4composite photocatalyst under simulated sunlight, while the composite photocatalyst still maintained extremely high degradation performance in cycling tests.

Direct Growth of Feather-Like ZnO Structures by a Facile Solution Technique for Photo-Detecting Application.

The feather-like hierarchical zinc oxide (ZnO) was synthesized via successive ionic layer adsorption and reaction without any seed layer or metal catalyst. A possible growth mechanism is proposed to explain the forming process of ZnO feather-like structures. Meanwhile, the photo-electronic performances of the feather-like ZnO have been investigated with the UV-vis-NIR spectroscopy, I-V and I-tmeasurements. The results indicate that feather-like ZnO hierarchical structures have good anti-reflection and excellent photo-sensitivity. All results suggest that the direct growth processing of novel feather-like ZnO is envisaged to have promising application in the field of photo-detector devices.

Probing the binding of trypsin to glutathione-stabilized gold nanoparticles in aqueous solution.

We investigate the interaction of trypsin with glutathione-stabilized Au nanoparticles (NPs) using fluorescence, synchronous fluorescence and ultraviolet (UV) absorption spectroscopy. We find that trypsin binds strongly to the Au NPs with a static quenching mechanism, and that the interaction is characteristic of positive cooperative binding. Furthermore, we determine the binding constants and the thermodynamic parameters, which suggest that the main binding forces between the glutathione-stabilized Au NPs and trypsin are electrostatic interactions and hydrogen bonding. Analysis of UV-vis absorption spectra suggests that aggregation of the Au NPs occurs in the trypsin/Au NPs system, which significantly alters the conformation of the protein.