Chemically engineered hemoprotein toward artificial metalloenzymes and biomaterials
Koji Oohora
Graduate School of Engineering, Osaka University
Mardi 09/07/2024, 11:00-12:30
Bât. 125 - Salle de réunion 2e étage

Hemoprotein containing heme, an iron porphyrin, as a cofactor is a promising scaffold toward artificial metalloenzymes and functional materials due to the unique characteristics derived from the synergetic combination of the metal cofactor and protein matrix. In this context, our group has demonstrated artificial metalloenzymes constructed by insertion of an artificial metal cofactor into the heme-binding site of a simple hemoprotein. These engineered proteins show catalytic activities including C–H bond hydroxylation, C–H bond amination, olefin cyclopropanation, methyl transfer and methane evolution. As a material application, light harvesting systems have also been investigated by assembly of photosensitizer-containing oligomeric hemoprotein. Furthermore, a hydrogel containing engineered hemoprotein was recently constructed toward redox-responsive biomaterials.

1) K. Oohora, T. Hayashi, Dalton Trans. 2021, 50, 1940. 2) K. Oohora, H. Meichin, H. Sugimoto, Y. Shiro, T. Hayashi, J. Am. Chem. Soc. 2017, 139, 18460. 3) K. Oohora, N. Fujimaki, R. Kajihara, H. Watanabe, T. Uchihashi, T. Hayashi, J. Am. Chem. Soc. 2018, 140, 10145. 4) S. Hirayama, K. Oohora, T. Uchihashi, T. Hayashi, J. Am. Chem. Soc. 2020, 142, 1822. 5) Y. Kagawa, K. Oohora, T. Himiyama, A. Suzuki, T. Hayashi, Angew. Chem. Int. Ed. 2024, in press.

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