Proceedings of MATSUS Spring 2025 Conference (MATSUSSpring25)
DOI: https://doi.org/10.29363/nanoge.matsusspring.2025.319
Publication date: 16th December 2024
The synthetic tunability of electronic structure and surface chemistry of semiconductor nanocrystals make them attractive light absorbers for light-driven chemistry. In this talk, I will describe our collaborative work on coupling nanocrystals with the MoFe protein of nitrogenase for light-driven N2 reduction to ammonia. The focus will be on our efforts to understand how nanocrystal properties determine the binding interactions with the enzyme, how electron transfer from the nanocrystals to the enzyme to drive ammonia formation, and how this platform can be used for studies of MoFe catalysis mechanisms.
We have functionalized nanocrystals to guide electrostatic attachment to the MoFe protein. Studies of experimental determinants of photochemical formation of H2 and NH3 suggest that the high excitation rates achieved with nanocrystals allow for accumulation of sufficient electrons on the enzyme to drive NH3 production. Transient absorption studies of electron transfer kinetics suggest that electron transfer efficiency is limited at single particle level by the competition between relatively slower electron transfer and relatively faster electron-hole recombination. At the ensemble level, electron transfer efficiency is also limited by the strength of the binding interactions. Microscale thermophoresis studies reveal that the nanocrystal-enzyme binding is highly sensitive to the nanocrystal dimensions. Light-driven injection of electrons into MoFe protein has enabled electron paramagnetic studies of the enzyme catalytic cycle in these systems and the key results of those studies will be highlighted.
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