Single‐atom catalysts are promising platforms for heterogeneous catalysis, especially for clean energy conversion, storage, and utilization. Although great efforts have been made to examine the bonding and oxidation state of single‐atom catalysts before and/or after catalytic reactions, when information about dynamic evolution is not sufficient, the underlying mechanisms are often overlooked. Herein, we report the direct observation of the charge transfer and bond evolution of a single‐atom Pt/C3N4 catalyst in photocatalytic water splitting by synchronous illumination X‐ray photoelectron spectroscopy. Specifically, under light excitation, we observed Pt−N bond cleavage to form a Pt0 species and the corresponding C=N bond reconstruction; these features could not be detected on the metallic platinum‐decorated C3N4 catalyst. As expected, H2 production activity (14.7 mmol h−1 g−1) was enhanced significantly with the single‐atom Pt/C3N4 catalyst as compared to metallic Pt‐C3N4 (0.74 mmol h−1 g−1).

The correlation between the dielectric breakdown performance and interface polarization was studied by the measurements of the dielectric breakdown strength and impedance spectroscopy as a function of sintering temperatures in a BaO–SrO–TiO2–Al2O3–SiO2 glass ceramic system. It was found that dielectric breakdown strength strongly depends on the interface polarization. The sintering temperature dependence of breakdown strength is attributed to the variation in interfacial polarization based on the results of complex impedance analysis.

Single cell mass spectrometry (MS) is uniquely positioned for the sequencing and identification of peptides in rare cells. Small peptides can take on different roles in subcellular compartments. Whereas some peptides serve as neurotransmitters in the cytoplasm, they can also function as transcription factors in the nucleus. Thus, there is a need to analyze the subcellular peptide compositions in identified single cells. Here, we apply capillary microsampling MS with ion mobility separation for the sequencing of peptides in single neurons of the mollusk Lymnaea stagnalis, and the analysis of peptide distributions between the cytoplasm and nucleus of identified single neurons that are known to express cardioactive Phe-Met-Arg-Phe amide-like (FMRFamide-like) neuropeptides. Nuclei and cytoplasm of Type 1 and Type 2 F group (Fgp) neurons were analyzed for neuropeptides cleaved from the protein precursors encoded by alternative splicing products of the FMRFamide gene. Relative abundances of nine neuropeptides were determined in the cytoplasm. The nuclei contained six of these peptides at different abundances. Enabled by its relative enrichment in Fgp neurons, a new 28-residue neuropeptide was sequenced by tandem MS.

Mixing negatively charged carbon quantum dots with a zwitterionic surfactant in water produces a variety of supramolecular structures, which are photoluminescent and show a reversible response to pH.