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Improving the catalytic efficiency of platinum group metal-free (PGM-free) catalysts for the sluggish alkaline hydrogen oxidation reaction (HOR) is crucial to the anion exchange membrane fuel cell. Recently, numerous Ni-based heterostructures have been designed based on bifunctional theory to enhance HOR activity by optimizing the binding energy of both H* and OH*; however, their activities are still far inferior to those of PGM catalysts. Indeed, the long transfer pathway for intermediates between different active sites in such heterostructures has rarely been investigated, which could be the reason for the bottleneck. Here, we design a Ni/MoOxHyheterostructure catalyst to promote H* migration from the Ni side to the interface for alkaline HOR via the hydrogen spillover effect. In situ X-ray absorption fine structure, Raman characterizations, H/D kinetic isotope effects, and theoretical calculations have proven facile H* migration from the Ni side to the interface, which further reacts with OH* on the MoOxHysurface. Besides, the hydrogen spillover effect is also beneficial for the preservation of the metallic phase of Ni during the reaction. The catalyst exhibits a high activity with Jk,mof 58.5 mA mgNi–1and j0,sof 42 μA cmNi–2, which is among the best PGM-free catalysts and is even comparable to some PGM catalysts. It also shows the highest power density (511 mW cm–2) as a PGM-free anode when assembled into fuel cells under moderate back pressure. These findings prove that in addition to optimizing electrophilicity and oxophilicity for active sites, we could also improve the HOR activity from the transfer pathway for intermediates, which provides insight into the design of other efficient HOR catalysts.

At steady state, the NOD-like receptor (NLR)-containing pyrin domain (PYD) (NLRP)1 inflammasome is maintained in an auto-inhibitory complex by dipeptidyl peptidases 8 and 9 (DPP8 and DPP9) and is activated by pathogen-encoded proteases after infection. Here, we showed that the open reading frame (ORF)45 protein of the Kaposi’s sarcoma-associated herpesvirus activated the human NLRP1 (hNLRP1) inflammasome in a non-protease-dependent manner, and we additionally showed that the Linker1 region of hNLRP1, situated between the PYD and NACHT domains, was required for the auto-inhibition and non-protease-dependent activation of hNLRP1. At steady state, the interaction between Linker1 and the UPA subdomain silenced the activation of hNLRP1 in auto-inhibitory complexes either containing DPP9 or not in a manner independent of DPP9. ORF45 binding to Linker1 displaced UPA from the Linker1–UPA complex and induced the release of the C-terminal domain of hNLRP1 for inflammasome assembly. The ORF45-dependent activation of the NLRP1 inflammasome was conserved in primates but was not observed for murine NLRP1b inflammasomes.

The electrocatalytic urea oxidation reaction (UOR) provides a promising alternative to the oxygen evolution reaction (OER) for various renewable energy-related systems owing to its lower thermodynamic barriers. However, its optimization and commercial utilization were hampered due to a lack of mechanistic understanding. Here, we demonstrate a Ce-doped Ni3S2catalyst supported on Ni foam (Ce–Ni3S2/NF) with superior activity toward UOR. The resultant Ce–Ni3S2/NF catalyst exhibits a lower Tafel slope of 20.3 mV dec–1, a higher current density of 100 mA cm–2at 1.39 V versus RHE, and better durability than those for Ni3S2/NF. Based on in situ synchrotron radiation X-ray absorption spectroscopy, in situ Fourier transform infrared (FTIR), and in situ Raman spectroscopy, we observe the structural reconstruction of sulfide and identify the adsorbed intermediates during UOR. Density functional theory (DFT) calculations reveal that Ce can regulate the electronic structure of Ni through Ce(4f)–O(2p)–Ni(3d) orbital electronic coupling. The modulated Ni sites have weaker adsorption of carbonaceous intermediates, thus accelerating the UOR. This work provides a promising route for the design of high-activity UOR catalysts.

The ongoing coronavirus disease 2019 (COVID-19) pandemic caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) is a global public health concern due to relatively easy person-to-person transmission and the current lack of effective antiviral therapy. However, the exact molecular mechanisms of SARS-CoV-2 pathogenesis remain largely unknown.