New functionalization of myoglobin by chemical modification of heme-propionates

Takashi Hayashi, Yoshio Hisaeda

    Research output: Contribution to journalArticlepeer-review

    107 Citations (Scopus)


    The reconstitution of myoglobin with an artificially created prosthetic group is a unique method for introducing a new chemical function into the protein. Particularly, the modification of two heme-propionates gives us an effective binding domain or binding site on the protein surface. This Account traces the design and construction of the highly ordered binding domain around the entrance of the heme pocket. The discussion includes the protein-small molecule or protein-protein recognition, electron transfer reaction within the complex, and enhancement of the chemical reactivity of the myoglobin with a substrate binding site. The synthetic approach to modifying a protein will be a new trend in engineering a novel function in naturally occurring hemoprotein.

    Original languageEnglish
    Pages (from-to)35-43
    Number of pages9
    JournalAccounts of Chemical Research
    Issue number1
    Publication statusPublished - Jan 31 2002

    All Science Journal Classification (ASJC) codes

    • Chemistry(all)


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