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Title
Japanese:Hierarchical Assembly of Hemin-Peptide Catalytic Systems on Graphite Surfaces 
English:Hierarchical Assembly of Hemin-Peptide Catalytic Systems on Graphite Surfaces 
Author
Japanese: 杉山茉莉絵, Ayhan Yurtsever, Nina Uenodan, Yuta Nabae, Takeshi Fukuma, 早水裕平.  
English: Marie Sugiyama, Ayhan Yurtsever, Nina Uenodan, Yuta Nabae, Takeshi Fukuma, Yuhei Hayamizu.  
Language English 
Journal/Book name
Japanese:ACS Nano 
English:ACS Nano 
Volume, Number, Page Vol. 19    No. 14    pp. 13760-13767
Published date Feb. 2025 
Publisher
Japanese:American Chemical Society 
English:American Chemical Society 
Conference name
Japanese: 
English: 
Conference site
Japanese: 
English: 
Official URL https://doi.org/10.1021/acsnano.4c15373
 
DOI https://doi.org/10.1021/acsnano.4c15373
Abstract The formation of molecular hybrid systems with cofactors and peptides on graphite electrodes has recently been demonstrated. The design of peptide sequences is crucial for forming robust catalytic molecular systems on electrodes. However, the relationship between peptide sequences, molecular structure, and catalytic performance has not been fully explored. In this study, we employed peptides with simple dipeptide repeats, which effectively immobilize hemin, to construct a stable catalytic system and investigated the molecular basis of their self-assembly and catalytic activity by varying the sequence. Among peptides containing the dipeptide sequences (YH, VH, and LH), YH demonstrated the most efficient immobilization of hemin, which is catalytically active in electrochemical reactions. Using advanced molecular visualization techniques, specifically frequency modulation atomic force microscopy (FM-AFM), we characterized the well-ordered structures of these peptides on graphite electrodes, revealing their molecular-scale organization. Our findings in electrochemical characterizations include a quantitative evaluation of the surface density of hemin immobilized by self-assembled peptides and the catalytic activity of the peptide-hemin hybrid system under electrochemical conditions in the presence of H2O2. The strong peptide窶菟eptide and peptide-hemin interactions, facilitated by ﾏ�窶苫� interactions of tyrosine residues, contribute to the system窶冱 stability and efficiency. The dipeptide repeats serve as a useful platform to investigate the role of important amino acids, beyond histidine, in stably immobilizing cofactors. These results highlight the potential for developing durable and efficient catalytic interfaces in electrochemical applications.

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