Extreme Functionalization of Hemoproteins upon the Direct Chemical Modification to Heme Framework

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The incorporation of an artificially created heme into an apohemoprotein is a unique method for introducing a new chemical function into a protein. In this project, we mainly focused on a modification of heme framework to improve the function and/or create a new function in myoglobin. The summary of our recent results are shown as follows:1.An iron porphycene as a structural isomer of the heme was inserted into apomyoglobin. The obtained reconstituted myoglobin showed an extremely high dioxygen affinity.2.The reconstituted myoglobin with the iron porphycene showed peroxidase/peroxygenase activity. In addition, the compound III formation in the presence of hydrogen peroxide was firstly observed in myoglobin. Furthermore, a hybrid myoglobin which was prepared by heme-propionate modification and amino-acid mutation showed high peroxidase activity and is a good catalyst toward bisphenol A degradation.3.Unusual dioxygen selectivity was obtained by introducing a hydrophobic cluster at the terminal two heme-propionate side chains.These results suggest that the replacement of native heme with an artificially created prosthetic group will serve as a new way to create a functionalized hemoprotein.