Dr. Kong

Hollow nanostructures have attracted increasing research interest in electrochemical energy storage and conversion owing to their unique structural features. However, the synthesis of hollow nanostructured metal phosphides, especially nonspherical hollow nanostructures, is rarely reported. Herein, we develop a metal–organic framework (MOF)-based strategy to synthesize carbon incorporated Ni–Co mixed metal phosphide nanoboxes (denoted as NiCoP/C). The oxygen evolution reaction (OER) is selected as a demonstration to investigate the electrochemical performance of the NiCoP/C nanoboxes. For comparison, Ni–Co layered double hydroxide (Ni–Co LDH) and Ni–Co mixed metal phosphide (denoted as NiCoP) nanoboxes have also been synthesized. Benefiting from their structural and compositional merits, the as-synthesized NiCoP/C nanoboxes exhibit excellent electrocatalytic activity and long-term stability for OER.

Box clever: ZIF-67@layered double hydroxide (LDH) nanoboxes are synthesized from highly uniform ZIF-67 nanocubes through reaction with Ni(NO₃)₂ at room temperature. After phosphidation with NaH₂PO₂, the ZIF-67@LDH nanoboxes are transformed into NiCoP/C nanoboxes, which have enhanced performance as an electrocatalyst for the oxygen evolution reaction (OER).

Biophysics under extreme conditions is the fundamental platform for scrutinizing life in unusual habitats, such as those in the deep sea or continental subsurfaces, but also for putative extraterrestrial organisms. Therefore, an important thermodynamic variable to explore is pressure. It is shown that the combination of infrared spectroscopy with simulation is an exquisite approach for unraveling the intricate pressure response of the solvation pattern of TMAO in water, which is expected to be transferable to biomolecules in their native solvent. Pressure-enhanced hydrogen bonding was found for TMAO in water. TMAO is a molecule known to stabilize proteins against pressure-induced denaturation in deep-sea organisms.

Squeeze it out of them: Trimethylamine N-oxide (TMAO) is known to stabilize protein structures at extreme pressures, possibly through hydrogen bonding. A combination of FTIR spectroscopy and computer simulation has now been used to connect pressure-induced changes in the IR spectrum of TMAO (see picture) to a locally enhanced hydrogen-bonding network at high compression. The insight gained should be transferable to biomolecules in their native solvent.