The B-type Channel is a Major Route for Iron Entry into the Ferroxidase Center and Central Cavity of Bacterioferritin

Wong, Steve, Grigg, Jason, Le Brun, Nick, Moore, Geoff, Murphy, Michael and Mauk, Grant (2015) The B-type Channel is a Major Route for Iron Entry into the Ferroxidase Center and Central Cavity of Bacterioferritin. The Journal of Biological Chemistry, 290 (6). pp. 3732-3739. ISSN 1083-351X

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Abstract

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 (N34, E66, D132, and D139) 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. 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.

Item Type: Article
Additional Information: Open Access with a Creative Commons Attribution Unported Licence
Uncontrolled Keywords: escherichia coli (e. coli),ferritin,iron,site-directed mutagenesis,x-ray crystallography,bacterioferritin,iron storage,iron core
Faculty \ School: Faculty of Science > School of Chemistry
Depositing User: Pure Connector
Date Deposited: 02 Feb 2015 15:52
Last Modified: 17 Sep 2020 23:59
URI: https://ueaeprints.uea.ac.uk/id/eprint/52073
DOI: 10.1074/jbc.M114.623082

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