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Photocurrent Generation from Hierarchical Zinc-Substituted Hemoprotein Assemblies Immobilized on a Gold Electrode

Authors

  • Dr. Akira Onoda,

    1. Department of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, 565-0871 (Japan)
    2. Frontier Research Base for Global Young Researchers, Graduate School of Engineering, Osaka University (Japan)
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  • Yasuaki Kakikura,

    1. Department of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, 565-0871 (Japan)
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  • Dr. Taro Uematsu,

    1. Department of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, 565-0871 (Japan)
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  • Prof. Dr. Susumu Kuwabata,

    1. Department of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, 565-0871 (Japan)
    2. Japan Science and Technology Agency, CREST, Kawaguchi, Saitama 332-0012 (Japan)
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  • Prof. Dr. Takashi Hayashi

    Corresponding author
    1. Department of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, 565-0871 (Japan)
    • Department of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, 565-0871 (Japan)
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  • This work was supported by Grants-in-Aid for Scientific Research ((B) and Innovative Areas “Coordination Programming”, area 2107) from MEXT, the Global COE Program of Osaka University, and the Japan Society for the Promotion of Science (JSPS). A.O. acknowledges a support from the Frontier Research Base for Global Young Researchers, Osaka University, on the Program of MEXT, and from the Ogasawara Foundation. T.H. acknowledges a support from the Asahi Grass Foundation.

Abstract

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All connected: A protein-immobilized electrode comprising hierarchical assemblies of photoactive cytochrome b562 reconstituted with zinc protoporphyrin IX exhibits remarkably enhanced photocurrent generation relative to an electrode bearing a single zinc-substituted hemoprotein layer. The protein oligomers, which bear a covalently linked protoporphyrin group, assemble by a supramolecular heme/heme pocket interaction.

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