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Title: The B-type channel is a major route for iron entry into the ferroxidase center and central cavity of bacterioferritin

Journal Article · · Journal of Biological Chemistry
 [1];  [1];  [2];  [2];  [1];  [1]
  1. Univ. of British Columbia, Vancouver, BC (Canada)
  2. Univ. of East Anglia, Norwich (United Kingdom)
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Bacterioferritin is a bacterial iron storage and detoxification protein that is capable of forming a ferric oxyhydroxide mineral core within its central cavity. To do this, iron must traverse the bacterioferritin protein shell, which is expected to occur through one or more of the channels through the shell identified by structural studies. The size and negative electrostatic potential of the 24 B-type channels suggest that they could provide a route for iron into bacterioferritin. Residues at the B-type channel (Asn-34, Glu-66, Asp-132, and Asp-139) of E. coli bacterioferritin were substituted to determine if they are important for iron core formation. A significant decrease in the rates of initial oxidation of Fe(II) at the ferroxidase center and subsequent iron mineralization was observed for the D132F variant. The crystal structure of this variant shows that substitution of residue 132 with phenylalanine caused a steric blockage of the B-type channel and no other material structural perturbation. Here, we conclude that the B-type channel is a major route for iron entry into both the ferroxidase center and the iron storage cavity of bacterioferritin.

Research Organization:
Univ. of British Columbia, Vancouver, BC (Canada); Univ. of East Anglia, Norwich (United Kingdom)
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER); National Inst. of Health (NIH) (United States); Canadian Foundation for Innovation (Canada); United Kingdom Biotechnology and Biological Sciences Research Council; Leverhulme Trust (United Kingdom); Natural Science and Engineering Research Council (Canada); Canadian Institutes of Health Research (Canada); Canadian Blood Services (Canada)
Grant/Contract Number:
83/B14704; BB/D001943/1; EM-2014-088
OSTI ID:
1349650
Journal Information:
Journal of Biological Chemistry, Vol. 290, Issue 6; ISSN 0021-9258
Publisher:
American Society for Biochemistry and Molecular BiologyCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 19 works
Citation information provided by
Web of Science

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Cited By (3)

Engineering Genetically-Encoded Mineralization and Magnetism via Directed Evolution journal November 2016
Routes of iron entry into, and exit from, the catalytic ferroxidase sites of the prokaryotic ferritin Syn Ftn journal January 2020
Engineering Genetically-Encoded Mineralization and Magnetism via Directed Evolution journal November 2016

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Related Subjects

59 BASIC BIOLOGICAL SCIENCES
Escherichia coli (E. coli)
ferritin
iron
site-directed mutagenesis
X-ray crystallography
bacterioferritin
iron storage
iron core