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• W4220844800 abstract "The molecular integration details such as protein orientation, interfacial microdomains, and overall structure modulation of photosystem II-semiconductor hybrids which exhibit great potential in solar-to-chemical energy conversion are systematically interrogated by lysine reactivity profiling mass spectrometry. Semi-artificial photosynthesis interfacing catalytic protein machinery with synthetic photocatalysts exhibits great potential in solar-to-chemical energy conversion. However, characterizing and manipulating the molecular integration structure at the biotic-abiotic interface remain a challenging task. Herein, the biointerface molecular integration details of photosystem II (PSII)-semiconductor hybrids, including the PSII orientation, interfacial microdomains, and overall structure modulation, are systematically interrogated by lysine reactivity profiling mass spectrometry. We demonstrate the semiconductor surface biocompatibility is essential to the PSII self-assembly with uniform orientation and electroactive structure. Highly directional localization of PSII onto more hydrophilic Ru/SrTiO 3 :Rh surface exhibits less disturbance on PSII structure and electron transfer chain, beneficial to the high water splitting activity. Further, rational modification of hydrophobic Ru 2 S 3 /CdS surface with biocompatible protamine can improve the hybrid O 2 -evolving activity 83.3%. Our results provide the mechanistic understanding to the structure–activity relationship of PSII-semiconductor hybrids and contribute to their rational design in the future." @default.
• W4220844800 created "2022-04-03" @default.
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• W4220844800 date "2022-07-01" @default.
• W4220844800 modified "2023-09-28" @default.
• W4220844800 title "Characterization and manipulation of the photosystem II-semiconductor interfacial molecular interactions in solar-to-chemical energy conversion" @default.
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• W4220844800 doi "https://doi.org/10.1016/j.jechem.2022.03.002" @default.
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