Molecular Assembly of Zinc Chlorophyll Derivatives by Using Recombin ant Light-Harvesting Polypeptides with His-tag and Immobilization on a Gold Electrode
Molecular Assembly of Zinc Chlorophyll Derivatives by Using Recombin ant Light-Harvesting Polypeptides with His-tag and Immobilization on a Gold Electrode
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利用带组氨酸标签的重组蚂蚁光捕获多肽分子组装并固定在金电极上的叶绿素锌衍生物
DOI:
10.1021/la400059h
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发表时间:
2013
期刊:
影响因子:
3.9
通讯作者:
Hideki Hashimoto and Mamoru Nango
中科院分区:
文献类型:
--
作者:
Shunsuke Sakai;Ibmoyasu Noji;Masaharu Kondo;Toshihisa Mizuno;Takehisa Dewa;Tsuyoshi Ochiai;Hisanori Yamakawa;Shigeru Itoh;Hideki Hashimoto and Mamoru Nango
LH1-α and -β 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-α variant, which has a His-tag at the C-terminus (MBP-rubα-YH). Zn-Chlorin and the Zn-Chlorin dimer could bind to MBP-rubα-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-α polypeptides but also suggest a clue to construct artificial photosynthesis systems using these peptide materials.