Crystal structure of bacterioferritin from Rhodobacter sphaeroides

Ki Hyun Nam, Yongbin Xu, Shunfu Piao, Amit Priyadarshi, Eun Hye Lee, Hye Yeon Kim, Young Ho Jeon, Nam Chul Ha, Kwang Yeon Hwang

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)


Iron is essential for the survival of organisms, but either excess or deficient levels of iron induce oxidative stress, thereby causing cell damage. As a result, iron regulation is essential for proper cell growth and proliferation in most organisms. Bacterioferritin is a ferritin-like family protein that contains a heme molecule and a ferroxidase site at the di-iron center. This protein plays a primary role in intracellular iron storage for iron homeostasis, as well as in the maintenance of iron in a soluble and non-toxic form. Although several bacterioferritin structures have been determined, no structural studies have successfully elucidated the molecular function of the heme molecule and the ferroxidase center. Here, we report the crystal structure of bacterioferritin from Rhodobacter sphaeroides. This protein exists in a roughly spherical configuration via the assembly of 24 subunits. We describe the oligomeric arrangement, ferroxidase center and heme-binding site based on this structure. The protein contains a single iron-binding configuration in the ferroxidase center, which allows for the release of iron by His130 when the protein is in the intermediate state. The heme molecule in RsBfr is stabilized by shifting of the van der Waals interaction center between the porphyrin of the heme and Trp26. We anticipate that further structural analysis will provide a more complete understanding of the molecular mechanisms of members of the ferritin-like family.

Original languageEnglish
Pages (from-to)990-994
Number of pages5
JournalBiochemical and biophysical research communications
Issue number1
Publication statusPublished - 2010 Jan 1

Bibliographical note

Funding Information:
We thank the staff for their assistance during the data collection at Beamline 4A of the Pohang Light Source, Korea. This study was supported by the Functional Proteomics Center , 21C Frontier Program, of the Korea Ministry of Science and Technology and the K-MeP of Korea Basic Science Institute. K.H. Nam was supported by a Research Fellowship from the BK21 Project.


  • Bacterioferritin
  • Crystal structure
  • Ferritin family
  • Ferroxidase center
  • Heme binding

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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