Graphitic carbon nitride (g-C 3 N 4 ), a polymeric semiconductor, has become a rising star for photocatalytic energy conversion because of its facile accessibility, metal-free nature, low cost, and environmentally benign properties. This work reviews the latest progress of g-C 3 N 4 -based materials in visible-light-driven water splitting to hydrogen. It begins with a brief history of g-C 3 N 4 , followed by various engineering strategies of g-C 3 N 4 , such as elemental doping, copolymerization, crystalline tailoring, surface engineering, and single-atom modification, for elevated photocatalytic water decomposition. In addition, the synthesis of g-C 3 N 4 in different dimensions (0D, 1D, 2D, and 3D) and configurations of a series of g-C 3 N 4based heterojunctions (type II, Z-scheme, S-scheme, g-C 3 N 4 /metal, and g-C 3 N 4 /carbon heterojunctions) were also discussed for their improvement in photocatalytic hydrogen production. Lastly, the challenges and opportunities of g-C 3 N 4 -based nanomaterials are provided. It is anticipated that this review will promote the further development of the emerging g-C 3 N 4 -based materials for more efficiency in photocatalytic water splitting to hydrogen.

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Actin binding compounds are widely used tools in cell biology. We compare the biological and biochemical effects of miuraenamide A and jasplakinolide, a structurally related prototypic actin stabilizer. Though both compounds have similar effects on cytoskeletal morphology and proliferation, they affect migration and transcription in a distinctive manner, as shown by a transcriptome approach in endothelial cells. In vitro , miuraenamide A acts as an actin nucleating, F-actin polymerizing and stabilizing compound, just like described for jasplakinolide. However, in contrast to jasplakinolide, miuraenamide A competes with cofilin, but not gelsolin or Arp2/3 for binding to F-actin. We propose a binding mode of miuraenamide A, explaining both its similarities and its differences to jasplakinolide. Molecular dynamics simulations suggest that the bromophenol group of miurenamide A interacts with residues Tyr133, Tyr143, and Phe352 of actin. This shifts the D-loop of the neighboring actin, creating tighter packing of the monomers, and occluding the binding site of cofilin. Since relatively small changes in the molecular structure give rise to this selectivity, actin binding compounds surprisingly are promising scaffolds for creating actin binders with specific functionality instead of just “stabilizers”.