Self-assembly of one- and two-dimensional hemoprotein systems by polymerization through heme-heme pocket interactions.
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).
Kitagishi
Hiroaki
H
Department of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita 565-0871, Japan.
Kakikura
Yasuaki
Y
Yamaguchi
Hiroyasu
H
Oohora
Koji
K
Harada
Akira
A
Hayashi
Takashi
T
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
D006418:Heme; D045303:Cytochromes b