The use of ammonia as a hydrogen carrier has received much attention due to its high hydrogen content and liquid state under mild conditions, which could lead to fuel cell applications. This study demonstrates facile ammonia decomposition on ruthenium nanoparticles loaded on inorganic electride, C12A7:e⁻. A high turnover frequency (∼12 s⁻¹ at 400 °C) and low activation energy (64 kJ mol⁻¹) for recombinative N₂ desorption were obtained for Ru/C12A7:e⁻. N₂-temperature programmed desorption (N₂-TPD) and kinetic analyses indicate that the high catalytic performance is due to the low work function of chemically stable C12A7:e⁻, which enables electron injection to the antibonding orbital of the Ru–N bond formed transiently through the reaction by raising the Fermi level of Ru metal.

Glycosylation plays crucial regulatory roles in various biological processes such as development, immunity, and neural functions. For example, α1,3-fucosylation, the addition of a fucose moiety abundant in Drosophila neural cells, is essential for neural development, function, and behavior. However, it remains largely unknown how neural-specific α1,3-fucosylation is regulated. In the present study, we searched for genes involved in the glycosylation of a neural-specific protein using a Drosophila RNAi library. We obtained 109 genes affecting glycosylation that clustered into nine functional groups. Among them, members of the RNA regulation group were enriched by a secondary screen that identified genes specifically regulating α1,3-fucosylation. Further analyses revealed that an RNA–binding protein, second mitotic wave missing (Swm), upregulates expression of the neural-specific glycosyltransferase FucTA and facilitates its mRNA export from the nucleus. This first large-scale genetic screen for glycosylation-related genes has revealed novel regulation of fucTA mRNA in neural cells. Glycosylation plays crucial regulatory roles in various biological processes such as development, immunity, and neural functions. Accordingly, some glycans are generated in a stage- and tissue-specific manner. To address how such distinct glycosylation is regulated in different tissues, we performed a large-scale screen for genes involved in glycosylation of a neural-specific protein. We identified 109 genes, 95 of which are assigned for the first time as directly or indirectly involved in glycosylation. We further found that neural-specific glycosylation is regulated at the RNA level, which is a novel regulatory mechanism of tissue-specific glycosylation.