Enhancing the compatibility of the amyloid-dye hybrid nanostructure for improved photo-biocatalysis
作者机构:College of ChemistrySichuan UniversityChengdu 610064SichuanChina Analytical&Testing CentreState Key Laboratory of Hydraulics and Mountain River EngineeringSichuan UniversityChengdu 610064SichuanChina College of Biomass Science and EngineeringSichuan UniversityChengdu 610064SichuanChina School of Chemistry and Chemical EngineeringHenan Normal UniversityXinxiang 453007HenanChina
出 版 物:《Journal of Energy Chemistry》 (能源化学(英文版))
年 卷 期:2023年第78卷第3期
页 面:430-437,I0012页
核心收录:
学科分类:081705[工学-工业催化] 07[理学] 070205[理学-凝聚态物理] 08[工学] 0817[工学-化学工程与技术] 080501[工学-材料物理与化学] 0805[工学-材料科学与工程(可授工学、理学学位)] 0702[理学-物理学]
基 金:financial support from the National Natural Science Foundation of China(22274102 and 22001182) the Sichuan Science and Technology Program(2022ZYD0027) the Open Research Fund of School of Chemistry and Chemical Engineering,Henan Normal University(2022A02) the Fundamental Research Funds for the Central Universities
主 题:Photo-biocatalysis Dye-protein assembly Insulin amyloid ThT Compatibility
摘 要:Artificial photosynthesis is significant for renewable energy generation,sustainable development,and environmental ***-protein hybrids are promising for developing photosynthesis mimics(e.g.,photo-biocatalysis),but their performances are far lower than the plant photosystems,partially because of the incompatibility between dye and the protein matrix that limits excited state electron transfer of the included ***,using ThT-insulin amyloid assembly as a model system,we proposed that increasing the dye-protein compatibility could lead to the improved photo-biocatalytic performance.A ThT derivative,ThTPD,was designed with the same electron acceptor but extended π-conjugated donor *** integrated into the insulin amyloid,the extended π-conjugated donor structure allowed increased binding affinity and energy with the amyloid matrix,thus better electron transport to the mediator to drive the photocatalytic ***,compared with ThT, ThTPD exhibited improved light absorption and longer excited state *** photo-biocatalytic performance of ThTPD-insulin amyloid was greatly improved as compared with that of ThT in reduced nicotinamide adenine dinucleotide(NADH) *** integrating with NADH-dependent L-glutamate reductase,the efficiency of the ThTPD-insulin amyloid hybrid was 2.8-fold higher than that of ThT in glutamate generation,showing promising feature in biocatalytic solar-to-chemical conversion.