Synthetic peptides are an attractive candidate for the assembly of biomimetic redox catalysts. We have synthesized series of hemeprotein models (helichrome) which have structured polypeptides as a building unit. Four amphiphilic ahelices were attached to the porphyrin ring covalently so that they interacted with each other to form an a-helical bundle type conformation. Various mutants were also synthesized. The Zn(I1) Complex of the helichrome binds hydrophobic imidazoles selectively, indicating the existence of hydrophobic binding pocket(s) inside the molecule.