Self-assembly of hexameric hemoprotein chemically modified with functional molecules

摘要

In nature, many proteins provide various assemblies with unique functions derived from the sophisticated structures. Recently, artificial protein assemblies inspired by the natural ones have been focused on due to the significant potentials toward novel materials.1 In order to construct an artificial protein assembly, we employ the hexameric tyrosine-coordinated heme protein (HTHP) as a building block.2 It has a ring-shaped homohexameric structure and each monomer possesses one heme molecule. In this work, the chemical modification of HTHP was carried out toward the construction of assembly (Fig. 1).