(574a) Exploring Protein-Nanocrystal Interfaces for Photoassisted Enzymatic Activity

With increasing demands for alternative sources of fuel, extensive research has focused on discovering methods to generate renewable energy from earth abundant resources. In recent years, a wide range of inorganic nanostructures with high surface areas and tunable band gaps have been synthesized and used as photocatalysts. In this talk, I will showcase our recent efforts to apply a bioinspired approach to tailor protein-nanoparticle interfaces for studying photoassisted redox activity. In order to drive enzymatic reduction of dissolved gases, electron sources such as photocatalysts and electrochemistry have been studied. However, in order to optimize electron flow, there is a significant need to understand how the interface between the organic enzyme and inorganic semiconductor influences protein binding and dynamics. Many redox enzymes function through assembly of protein subunits utilizing complex and multivalent interactions, with binding strengths ranging from long-range and weak to short-range and near-covalent. Mimicking such exquisite binding motifs is likely to be key for replacing protein subunits with photoactive semiconductors. This talk will showcase our recent insight into the design of interfaces between semiconductor surfaces and proteins to control binding and conformational dynamics of enzymes to promote photodriven redox catalytic activities.