Molecular Assembly of Zinc Chlorophyll Derivatives by Using Recombinant Light-Harvesting Polypeptides with His-tag and Immobilization on a Gold Electrode

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• 作者：Shunsuke Sakai ; Tomoyasu Noji ; Masaharu Kondo ; Toshihisa Mizuno ; Takehisa Dewa ; Tsuyoshi Ochiai ; Hisanori Yamakawa ; Shigeru Itoh ; Hideki Hashimoto ; Mamoru Nango
• 刊名：Langmuir
• 出版年：2013
• 出版时间：April 30, 2013
• 年：2013
• 卷：29
• 期：17
• 页码：5104-5109
• 全文大小：283K
• 年卷期：v.29,no.17(April 30, 2013)
• ISSN：1520-5827

文摘

LH1-伪 and -尾 polypeptides, which make up the light-harvesting 1 (LH1) complex of purple photosynthetic bacteria, along with bacteriochlorophylls, have unique binding properties even for various porphyrin analogs. Herein, we used the porphyrin analogs, Zn-Chlorin and the Zn-Chlorin dimer, and examined their binding behaviors to the LH1-伪 variant, which has a His-tag at the C-terminus (MBP-rub伪-YH). Zn-Chlorin and the Zn-Chlorin dimer could bind to MBP-rub伪-YH and form a subunit-type assembly, similar to that from the native LH1 complex. These complexes could be immobilized onto Ni-nitrilotriacetic acid-modified Au electrodes, and the cathodic photocurrent was successfully observed by photoirradiation. Since Zn-Chlorins in this complex are too far for direct electron transfer from the electrode, a contribution of polypeptide backbone for efficient electron transfer was implied. These findings not only show interesting properties of LH1-伪 polypeptides but also suggest a clue to construct artificial photosynthesis systems using these peptide materials.