Supramolecular Assembling System Based on Apo-form ofHexameric Tyrosine-coordinated Heme Protein and EngineeredCytochrome b_(562)

摘要

Biological and chemical strategies have been used to create supramolecular proteinassemblies.The biological strategy focuses on protein-protein interaction found in naturalsystems such as employing naturally symmetrical proteins as building blocks to induce variousprotein nanostructures.Chemical strategy utilizes interactions between small molecules suchas protein-ligand (heme cofactor) and host-guest intearctions.In this decade,our group hasdemonstrated supramolecular hemoprotein assemblies via the protein-heme cofactorinteraction.A series of hemoprotein assembling systems have been constructed by the surfacemodification of cytochrome b562 mutant with synthetic heme via a covalent bond on its surface.This modified protein forms the linear supramolecular assembly by successive heme-hemepocket interactions.This work attempted the conjugation of this cytochrome b562assembly withan apo-form of a ring-shaped hexameric hemoprotein (HTHP) to construct a branchedsupramolecular system (Figure 1).