The overall water splitting efficiency is mainly restricted by the slowkinetics of oxygen evolution. Therefore,it is essential to develop active oxygen evolution catalysts.Inthis context, we designed and synthesized atungsten oxide catalyst with oxygen vacancies for photocatalytic oxygen evolution, which exhibited ah igher oxygen evolution rate of 683 mmol h À1 g À1 than that of pure WO 3 (159 mmol h À1 g À1). Subsequent studies through transient absorption spectroscopy found that the oxygen vacancies can produce electron trapping states to inhibit the direct recombination of photogenerated carriers.Additionally,aPt cocatalyst can promote electron trap states to participate in the reaction to improve the photocatalytic performance further.T his work uses femtosecond transient absorption spectroscopytoexplain the photocatalytic oxygen evolution mechanism of inorganic materials and provides new insights into the design of high-efficiency watersplitting catalysts.

The crystal structure of the bacterioferritin from Azotobacter vinelandii has been determined at 2.6 A resolution. Both the low occupancy of one iron ion in the dinuclear iron center and the deviation of its adjacent residue His130 from the center suggest migration of the iron ion from the dinuclear iron site to the inner nucleation site. The concerted movement of His130 and Glu47 may admit a dynamic gating mechanism for shift of the oxidized iron ion. Ba 2þ binding to the fourfold channel implicates that the channel bears Fe 2þ conductivity and selectivity to provide a route for iron access to the inner cavity during core formation.

Herein, we first reported a facile strategy to prepare functional Poly(vinyl alcohol) (PVA) hybrid film with well ultraviolet (UV) shielding property and visible light transmittance using graphene oxide nanosheets as UV-absorber. The absorbance of ultraviolet light at 300 nm can be up to 97.5%, while the transmittance of visible light at 500 nm keeps 40% plus. This hybrid film can protect protein from UVA light induced photosensitive damage, remarkably.

Golgin45 is required for normal Golgi structure and the transportation of protein from the ER. It forms a specific complex with GRASP55 Little is known regarding the molecular details of this interaction and its structural role in stacking of the Golgi complex. Here, we present the crystal structure of the GRASP domains of GRASP55 in complex with the Golgin45 C-terminal peptide, determined at 1.33 Å resolution. Similar to the structure of GRASP65 bound to GM130 reported recently, this structure reveals more than one interacting site and involves both PDZ1 and PDZ2 domains of the GRASP simultaneously. The C-terminal peptides of Golgin45 and GM130 present a conserved PDZ domain binding motif sequence and recognize the canonical PDZ-peptide binding groove of the PDZ1 domains of GRASP55 and GRASP65. A main difference in this recognition process resides in a structural rearrangement of GRASP65-GM130 that does not occur for the GRASP55-Golgin45 complex. The binding site at the cleft between the PDZ1 and PDZ2 domains of GRASP65 is dominated by hydrophobic interactions with GM130 that are not observed in the GRASP55-Golgin45 complex. In addition, a unique zinc finger structure is revealed in the GRASP55-Golgin45 complex crystal structure. Mutagenesis experiments support these structural observations and demonstrate that two of these sites are required to form a stable complex. Finally, a novel Golgi stacking model is proposed according to these structural findings.