Communication

Self-Assembly of One- and Two-Dimensional Hemoprotein Systems by Polymerization through Heme–Heme Pocket Interactions†

  1. Hiroaki Kitagishi Dr.1,3,
  2. Yasuaki Kakikura1,
  3. Hiroyasu Yamaguchi Dr.2,
  4. Koji Oohora1,
  5. Akira Harada Prof. Dr.2,
  6. Takashi Hayashi Prof. Dr.1

Article first published online: 3 DEC 2008

DOI: 10.1002/anie.200804006

Issue

Angewandte Chemie International Edition

Angewandte Chemie International Edition

Volume 48, Issue 7, pages 1271–1274, February 2, 2009

Additional Information

How to Cite

Kitagishi, H., Kakikura, Y., Yamaguchi, H., Oohora, K., Harada, A. and Hayashi, T. (2009), Self-Assembly of One- and Two-Dimensional Hemoprotein Systems by Polymerization through Heme–Heme Pocket Interactions. Angew. Chem. Int. Ed., 48: 1271–1274. doi: 10.1002/anie.200804006

Author Information

  1. 1

    Department of Applied Chemistry, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita 565-0871 (Japan), Fax: (+81) 6-6879-7930

  2. 2

    Department of Macromolecular Science, Graduate School of Science, Osaka University, Toyonaka 560-0043 (Japan)

  3. 3

    Present address: Department of Molecular Chemistry and Biochemistry, Doshisha University, Kyotanabe, Kyoto 610-0321 (Japan)

  1. †

    This work was supported by Grants-in-Aid for Scientific Research from MEXT. T.H. acknowledges a research grant from the Asahi Glass Foundation. H.K. was financially supported as an Inoue Fellow of the Inoue Foundation for Science.

Publication History

  1. Issue published online: 28 JAN 2009
  2. Article first published online: 3 DEC 2008
  3. Manuscript Revised: 14 OCT 2008
  4. Manuscript Received: 13 AUG 2008

Funded by

  • MEXT

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Keywords:

  • cytochrome b562;
  • heme proteins;
  • protein modifications;
  • self-assembly;
  • supramolecular chemistry

Abstract

Thumbnail image of graphical abstract

Supramolecular protein polymers: When a heme moiety was introduced to the surface of an apo-cytochrome b562(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).

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