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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

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.
Authors:
 [1] ;  [1] ;  [2] ;  [2] ;  [1] ;  [1]
  1. Univ. of British Columbia, Vancouver, BC (Canada)
  2. Univ. of East Anglia, Norwich (United Kingdom)
Publication Date:
Grant/Contract Number:
83/B14704; BB/D001943/1; EM-2014-088
Type:
Accepted Manuscript
Journal Name:
Journal of Biological Chemistry
Additional Journal Information:
Journal Volume: 290; Journal Issue: 6; Journal ID: ISSN 0021-9258
Publisher:
American Society for Biochemistry and Molecular Biology
Research Org:
Univ. of British Columbia, Vancouver, BC (Canada); Univ. of East Anglia, Norwich (United Kingdom)
Sponsoring Org:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22); USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23); 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)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; Escherichia coli (E. coli); ferritin; iron; site-directed mutagenesis; X-ray crystallography; bacterioferritin; iron storage; iron core
OSTI Identifier:
1349650

Wong, Steve G., Grigg, Jason C., Le Brun, Nick E., Moore, Geoffrey R., Murphy, Michael E. P., and Mauk, A. Grant. The B-type channel is a major route for iron entry into the ferroxidase center and central cavity of bacterioferritin. United States: N. p., Web. doi:10.1074/jbc.M114.623082.
Wong, Steve G., Grigg, Jason C., Le Brun, Nick E., Moore, Geoffrey R., Murphy, Michael E. P., & Mauk, A. Grant. The B-type channel is a major route for iron entry into the ferroxidase center and central cavity of bacterioferritin. United States. doi:10.1074/jbc.M114.623082.
Wong, Steve G., Grigg, Jason C., Le Brun, Nick E., Moore, Geoffrey R., Murphy, Michael E. P., and Mauk, A. Grant. 2014. "The B-type channel is a major route for iron entry into the ferroxidase center and central cavity of bacterioferritin". United States. doi:10.1074/jbc.M114.623082. https://www.osti.gov/servlets/purl/1349650.
@article{osti_1349650,
title = {The B-type channel is a major route for iron entry into the ferroxidase center and central cavity of bacterioferritin},
author = {Wong, Steve G. and Grigg, Jason C. and Le Brun, Nick E. and Moore, Geoffrey R. and Murphy, Michael E. P. and Mauk, A. Grant},
abstractNote = {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.},
doi = {10.1074/jbc.M114.623082},
journal = {Journal of Biological Chemistry},
number = 6,
volume = 290,
place = {United States},
year = {2014},
month = {12}
}