title: Self-assembly of one- and two-dimensional hemoprotein systems by polymerization through heme-heme pocket interactions.
abstract: Supramolecular protein polymers: When a heme moiety was introduced to the surface of an apo-cytochrome b(562)(H63C) mutant, supramolecular polymers formed through noncovalent heme-heme pocket interactions. The incorporation of a heme triad as a pivot molecule in the protein polymer further led to a two-dimensional protein network structure, which was visualized by tapping-mode atomic force microscopy (see picture).
authors.affiliation: Department of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita 565-0871, Japan.
authors.forename: Hiroaki
authors.initials: H
authors.lastname: Kitagishi
authors.forename: Yasuaki
authors.initials: Y
authors.lastname: Kakikura
authors.forename: Hiroyasu
authors.initials: H
authors.lastname: Yamaguchi
authors.forename: Koji
authors.initials: K
authors.lastname: Oohora
authors.forename: Akira
authors.initials: A
authors.lastname: Harada
authors.forename: Takashi
authors.initials: T
authors.lastname: Hayashi
mesh_terms: D045303:Cytochromes b / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D006418:Heme / Q000031:analogs & derivatives / Q000737:chemistry* / Q000378:metabolism*; D007536:Isomerism; D018625:Microscopy, Atomic Force; D009154:Mutation; D011485:Protein Binding; D011487:Protein Conformation; D054730:Protein Interaction Domains and Motifs
chemical_list: D006418:Heme; D045303:Cytochromes b