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Metal sulfides such as MoS 2 can serve as co-catalysts to greatly promote the overall efficiency of Fe 2+ -catalyzed advanced oxidation processes (AOPs). Unsaturated S atoms on the surface of metal sulfides can capture protons from the solution to form H 2 S and at the same time expose reductive metallic active sites to greatly accelerate the rate-limiting step of Fe 3+ /Fe 2+ conversion. The significantly enhanced efficiency of H 2 O 2 decomposition makes the AOPs viable for practical applications in the remediation of organic pollutants.

This study developed a facile approach for preparing Ti3+ self-doped TiO2-graphene photocatalyst by a one-step vacuum activation technology involved a relative lower temperature, which could be activated by the visible light owing to the synergistic effect among Ti3+ doping, some new intersurface bonds generation and graphene oxide reduction. Compared with the traditional methods, the vacuum activation involves a low temperature and low-costing, which can achieve the reduction of GO, the self doping of Ti3+ in TiO2 and the loading of TiO2 nanoparticles on GR surface at the same time. These resulting TiO2-graphene composites show the high photodegradation rate of MO, high hydrogen evolution activity and excellent IPCE in the visible light irradiation. The facile vacuum activation method can provide an effective and practical approach to improve the performance of TiO2-graphene and other metal oxides-graphene towards their practical photocatalytic applications.

Human FBP21 (formin-binding protein 21) contains a matrin-type zinc finger and two tandem WW domains. It is a component of the spliceosomes and interacts with several established splicing factors. Here we demonstrate for the first time that FBP21 is an activator of pre-mRNA splicing in vivo and that its splicing activation function and interaction with the splicing factor SIPP1 (splicing factor that interacts with PQBP1 and PP1) are both mediated by the two tandem WW domains of group III. We determined the solution structure of the tandem WW domains of FBP21 and found that the WW domains recognize peptide ligands containing either group II (PPLP) or group III (PPR) motifs. The binding interfaces involve both the XP and XP2 grooves of the two WW domains. Significantly, the tandem WW domains of FBP21 are connected by a highly flexible region, enabling their simultaneous interaction with two proline-rich motifs of SIPP1. The strong interaction between SIPP1 and FBP21 can be explained by the conjugation of two low affinity interactions with the tandem WW domains. Our study provides a structural basis for understanding the molecular mechanism underlying the functional implication of FBP21 and the biological specificity of tandem WW domains.Gene expression in eukaryotic cells involves several steps, including transcription, mRNA processing, and export. Pre-mRNA splicing takes place in the spliceosome, a highly dynamic ribonucleoprotein particle that consists of five small nuclear RNAs and at least 150 proteins. Small nuclear ribonucleoproteins (snRNPs) 3 and numerous protein factors are essential for the formation of the active spliceosome (1, 2). In budding yeast, the splicing factor Prp40 participates in crossintron bridging by interacting with the branch point-binding protein (BBP) and the U5 snRNP component Prp8. Prp40 contacts the 5Ј splice site and interacts with BBP, bringing the 5Ј splice site and the branch point in spatial proximity. These interactions are believed to be conserved in mammals (3-5). FBP21 (formin-binding protein 21), the mammalian Prp40-like protein, colocalizes with splicing factors in nuclear storage sites for pre-mRNA splicing factors. In addition, FBP21 is a component of the mammalian spliceosomal A/B complex and is associated with U2 snRNPs (6). FBP21 interacts directly with the splicing factors U1 snRNP protein U1C, the core snRNP proteins SmB and SmBЈ, and the branch point-binding protein SF1/mBBP, suggesting that it may also play a role in crossintron bridging of U1 and U2 snRNPs in the spliceosomes. FBP21 contains a matrin-type zinc finger and two group III WW domains ( Fig. 1) that are structurally related to those of the established splicing factors U1C and Prp40, respectively (6, 7). The binding of FBP21 to splicing factors is mediated by its tandem WW domains, which represent interaction modules for proline-rich ligands (4, 8, 9). Although the above data strongly suggest that FBP21 has a role in pre-mRNA splicing, there are no in vivo data to support this contention. The splicing...