33 research outputs found

    Highly Ordered Periodic Au/TiO<sub>2</sub> Hetero-Nanostructures for Plasmon-Induced Enhancement of the Activity and Stability for Ethanol Electro-oxidation

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    The catalytic electro-oxidation of ethanol is the essential technique for direct alcohol fuel cells (DAFCs) in the area of alternative energy for the ability of converting the chemical energy of alcohol into the electric energy directly. Developing highly efficient and stable electrode materials with antipoisoning ability for ethanol electro-oxidation remains a challenge. A highly ordered periodic Au-nanoparticle (NP)-decorated bilayer TiO<sub>2</sub> nanotube (BTNT) heteronanostructure was fabricated by a two-step anodic oxidation of Ti foil and the subsequent photoreduction of HAuCl<sub>4</sub>. The plasmon-induced charge separation on the heterointerface of Au/TiO<sub>2</sub> electrode enhances the electrocatalytic activity and stability for the ethanol oxidation under visible light irradiation. The highly ordered periodic heterostructure on the electrode surface enhanced the light harvesting and led to the greater performance of ethanol electro-oxidation under irradiation compared with the ordinary Au NPs-decorated monolayer TiO<sub>2</sub> nanotube (MTNT). This novel Au/TiO<sub>2</sub> electrode also performed a self-cleaning property under visible light attributed to the enhanced electro-oxidation of the adsorbed intermediates. This light-driven enhancement of the electrochemical performances provides a development strategy for the design and construction of DAFCs

    Universal Stress Protein Regulates Electron Transfer and Superoxide Generation Activities of the Cytochrome <i>bc</i><sub>1</sub> Complex from <i>Rhodobacter sphaeroides</i>

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    Interactions between <i>Rhodobacter sphaeroides</i> cytochrome <i>bc</i><sub>1</sub> complex (<i>Rsbc</i><sub>1</sub>) and soluble cytosolic proteins were studied by a precipitation pull-down technique. After being purified, detergent-dispersed <i>Rsbc</i><sub>1</sub> complex was incubated with soluble cytosolic fraction and then dialyzed in the absence of detergent; the interacting proteins were coprecipitated with <i>Rsbc</i><sub>1</sub> complex upon centrifugation. One of the cytosolic proteins pulled down by <i>Rsbc</i><sub>1</sub> complex was identified by liquid chromatography-coupled tandem mass spectrometry (LC/MS/MS) to be the reported <i>R. sphaeroides</i> universal stress protein (UspA). Incubating purified UspA with the detergent dispersed <i>bc</i><sub>1</sub> complex resulted in an increase in the <i>Rsbc</i><sub>1</sub> complex activity by 60% and a decrease in superoxide generation activity by the complex by more than 70%. These UspA effects were only observed with <i>Rsbc</i><sub>1</sub> complexes containing subunit IV and assayed under aerobic conditions. These results suggest that the interaction between UspA and <i>Rsbc</i><sub>1</sub> complex may play an important role in <i>R. sphaeroides</i> cells during oxidative stress. Using a biotin label transfer technique, cytochrome <i>c</i><sub>1</sub> of the <i>Rsbc</i><sub>1</sub> complex was identified as the interacting site for UspA
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