Electrocatalytic hydrogen and oxygen evolutions via water splitting are very demanding in the context of renewable energy and sustainable environment. We first report the synthesis of wormhole‐like mesoporous tin oxide (MTO‐S) by using sodium lauroyl sarcosinate as structure directing agent under hydrothermal reaction conditions followed by calcination and loading with IrO2 or Pt nanoparticles at its surface by simple wet‐chemical methods. These IrO2 and Pt‐loaded SnO2 nanomaterials are thoroughly characterized by small and wide‐angle powder XRD, nitrogen adsorption/desorption analysis, FTIR, XPS spectroscopy, UHR‐TEM, FE‐SEM, TG/DTA and NH3‐TPD analysis. The electrochemical water splitting measurements of the IrO2 and Pt doped mesoporous SnO2 nanostructured materials suggested fine dispersion of these metal/metal oxide nanoparticles at the mesopore surface and facile electron hopping could enhance the rate of the oxygen evolution reaction (OER) and hydrogen evolution reaction (HER) activity of IrO2@MTO‐S and Pt@MTO‐S nanocomposites, respectively. As a result, the IrO2@MTO‐S modified electrode exhibits unprecedented OER activity with a very low overpotential of 240 mV at 10 mA cm−2, which is lower than the state‐of‐the‐art catalyst IrO2/C (360 mV) and other reported catalysis. Pt@MTO‐S also exhibit excellent HER activity with an ultralow overpotential of 73 mV at 10 mA cm−2. These findings may uncover new opportunities for IrO2@MTO‐S and Pt@MTO‐S as OER and HER electrocatalysts for future water electrolysis.
The present work demonstrates a detailed characterization of the interaction of a potential chloride channel blocker, 9-methyl anthroate (9-MA), with a model transport protein, Bovine Serum Albumin (BSA). The modulated photophysical properties of the emissive drug molecule within the microheterogeneous bio-environment of the protein have been exploited spectroscopically to monitor the probe-protein binding interaction. Apart from evaluating the binding constant, the probable location of the neutral molecule within the protein cavity (subdomain IB) is explored by an AutoDock-based blind docking simulation. The absence of the Red-Edge Effect has been corroborated by the enhanced lifetime of the probe, being substantially greater than the solvent reorientation time. A dip-and-rise characteristic of the rotational relaxation profile of the drug within the protein has been argued to originate from a significant difference in the lifetime as well as amplitude of the free and protein-bound drug molecule. Unfolding of the protein in the presence of the drug molecule has been probed by the decrease of the α-helical content, obtained via circular dichroism (CD) spectroscopy, which is also supported by the gradual loss of the esterase activity of the protein in the presence of the drug molecule.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.