Preparation and O2 binding study of myoglobin having a cobalt porphycene

Takashi Matsuo, Takashi Tsuruta, Keiko Maehara, Hideaki Sato, Yoshio Hisaeda, Takashi Hayashi

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    40 Citations (Scopus)


    Sperm whale myoglobin, an oxygen-storage hemoprotein, was reconstituted with 2,7-diethyl-3,6,12,17-tetramethyl-13,16-bis(carboxyethyl) porphycenatocobalt(II) in order to investigate the reactivities of a cobalt porphycene in a protein matrix. Similar to the previously reported finding for the myoglobin with the iron porphycene, the reconstituted myoglobin with the cobalt porphycene was also found to have an O2 affinity 2 orders of magnitude greater than that of the myoglobin possessing cobalt protoporphyrin IX. The EPR spectra of the deoxy and oxy myoglobins having the cobalt porphycene at 77 K also have features similar to those of the myoglobin with cobalt protoporphyrin IX. These spectra suggest that the porphycene cobalt in the deoxy form is coordinated by one nitrogenous ligand postulated to be the imidazole ring of His93, and that the bond configuration of CoII-O2 is regarded as the CoIII-O2•- species.

    Original languageEnglish
    Pages (from-to)9391-9396
    Number of pages6
    JournalInorganic chemistry
    Issue number25
    Publication statusPublished - Dec 12 2005

    All Science Journal Classification (ASJC) codes

    • Physical and Theoretical Chemistry
    • Inorganic Chemistry


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