H 2 adsorption on Au catalysts is weak and reversible,m aking it difficult to quantitatively study.W e demonstrate H 2 adsorption on Au/TiO 2 catalysts results in electron transfer to the support, inducing shifts in the FTIR background. This broad background absorbance (BBA) signal is used to quantify H 2 adsorption;a dsorption equilibrium constants are comparable to volumetric adsorption measurements.H 2 adsorption kinetics measured with the BBAs how al ower E app value (23 kJ mol À1)f or H 2 adsorption than previously reported from proxy H/D exchange (33 kJ mol À1). We also identify ap reviously unreported H-O-H bending vibration associated with proton adsorption on electronically distinct Ti-OH metal-support interface sites,p roviding new insight into the nature and dynamics of H 2 adsorption at the Au/TiO 2 interface.
Subcellular stimulation by free radicals is crucial for deeper insight of cell behaviors. However, it remains a tough challenge due to the high spatial precision requirement and short life of radicals. Herein, we report a versatile open microfluidic probe for stable generation of free radical and subcellular stimulation. By optimizing parameters, the chemical reaction can be confined in a microregion with a diameter of several mm, and the real-time produced reactive radicals can attack the desired subcellular region of a single cell. In order to reveal the attacked region, fluorescent cyanine 3 labeled tyramide free radicals are synthesized, and the target microregion on a single cell is successfully stained by the covalent linking reaction between radicals and membrane proteins, which proves the feasibility of our method. We believe this method will open new avenues for short-lived reactive intermediates stimulation at the single-cell/sub-cell level and selective membrane labeling.
Proton-gated ion channels conduct mainly Na+ to induce postsynaptic membrane depolarization. Finding the determinants of ion selectivity requires knowledge of the pore structure in the open conformation, but such information is not yet available. Here, the open conformation of the hASIC1a channel was computationally modeled, and functional effects of pore mutations were analyzed in light of the predicted structures. The open pore structure shows two constrictions of similar diameter formed by the backbone of the GAS belt and, right beneath it, by the side chains of H28 from the reentrant loop. Models of nonselective mutant channels, but not those that maintain ion selectivity, predict enlargement of the GAS belt, suggesting that this motif is quite flexible and that the loss of stabilizing interactions in the central pore leads to changes in size/shape of the belt. Our results are consistent with the “close-fit” mechanism governing selectivity of hASIC1a, wherein the backbone of the GAS substitutes at least part of the hydration shell of a permeant ion to enable crossing the pore constriction.
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