Self-assembly of one- and two-dimensional hemoprotein systems by polymerization through heme-heme pocket interactions

Angew Chem Int Ed Engl. 2009;48(7):1271-4. doi: 10.1002/anie.200804006.

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).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cytochromes b / chemistry*
  • Cytochromes b / genetics
  • Cytochromes b / metabolism*
  • Cytochromes b / ultrastructure
  • Heme / analogs & derivatives
  • Heme / chemistry*
  • Heme / metabolism*
  • Isomerism
  • Microscopy, Atomic Force
  • Mutation
  • Protein Binding
  • Protein Conformation
  • Protein Interaction Domains and Motifs

Substances

  • Heme
  • Cytochromes b