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Supramolecular assembling systems of hemoproteins using chemical modifications

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Abstract

Inspired by protein assemblies in biological systems, various artificial protein assemblies have been constructed in these decades. Hemoprotein containing porphyrin iron complex, heme, is a unique building block of the artificial protein assemblies due to the structures, physicochemical properties and functions. In the case of hemoprotein containing b-type heme, the heme cofactor is non-covalently bound to the heme-binding site, heme pocket, in the protein matrix. This review summaries our efforts to utilize heme–heme pocket interactions toward supramolecular hemoprotein assembling systems with various structures and/or functions. Simple monomeric hemoprotein, mainly cytochrome b562, was employed as a useful building block and synthetic heme was attached to the cysteine-introduced variant to form a building block showing self-assembling behavior by interprotein heme–heme pocket interactions. The modulations of linker between synthetic heme and protein surface and/or protein modification site contribute to provide various structures such as fiber, ring, branched shape and micelles. Furthermore, hexameric hemoprotein was utilized for another building block with supramolecular approach toward light harvesting system by replacement of heme cofactors with porphyrinoid photosensitizers. A series of artificial hemoprotein assembling systems will contribute to new-type of functional biomaterials.

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Acknowledgements

The author appreciates the organizing committee of Host-Guest and Supramolecular Chemistry Society, Japan for giving him the SHGCS Japan Award of Excellence 2022 and the opportunity to write this review. The author also deeply thanks Prof. Takashi Hayashi of Osaka University for his positive and constructive suggestions. The coworkers who contributed to the results presented in this review are gratefully acknowledged as well as our collaborators. This work was funded by Grants-in-Aid for Scientific Research provided by JSPS KAKENHI Grant Numbers JP20H02755, JP20KK0315, and JP22H05364 and JST PPRESTO JPMJPR22A3. This is a paper selected for the "SHGSC Japan Award of Excellence 2022”.

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Authors and Affiliations

  1. Department of Applied Chemistry, Graduate School of Engineering, Osaka University, Suita, 565-0871, Japan

    Koji Oohora

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  1. Koji Oohora
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KO wrote the main manuscript text and prepared all of figures.

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Correspondence to Koji Oohora.

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Oohora, K. Supramolecular assembling systems of hemoproteins using chemical modifications. J Incl Phenom Macrocycl Chem 103, 97–107 (2023). https://doi.org/10.1007/s10847-023-01181-6

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