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Human Serum Albumin-Based Peroxidase Having an Iron Protoporphyrin IX in Artificial Heme Pocket

Authors

  • Kyohei Watanabe,

    1. Department of Applied Chemistry, Faculty of Science and Engineering, Chuo University, 1-13-27 Kasuga, Bunkyo-ku, Tokyo 112-8551 (Japan), Fax: (+81) 3-3817-1910
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  • Natsuki Ishikawa,

    1. Department of Applied Chemistry, Faculty of Science and Engineering, Chuo University, 1-13-27 Kasuga, Bunkyo-ku, Tokyo 112-8551 (Japan), Fax: (+81) 3-3817-1910
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  • Prof. Dr. Teruyuki Komatsu

    Corresponding author
    1. Department of Applied Chemistry, Faculty of Science and Engineering, Chuo University, 1-13-27 Kasuga, Bunkyo-ku, Tokyo 112-8551 (Japan), Fax: (+81) 3-3817-1910
    • Department of Applied Chemistry, Faculty of Science and Engineering, Chuo University, 1-13-27 Kasuga, Bunkyo-ku, Tokyo 112-8551 (Japan), Fax: (+81) 3-3817-1910

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Abstract

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Cooking up enzymes: Iron protoporphyrin IX (heme) is bound within a hydrophobic cavity in subdomain IB of human serum albumin (HSA). Site-specific mutations to introduce proximal and distal histidines into the heme pocket of HSA conferred a peroxidase activity to the prosthetic heme group. The catalytic activity of the recombinant HSA(mutant)–heme complex for guaiacol oxidation is 17-fold higher than that of HSA(wild type)–heme.

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