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Bradley, Justin M., Svistunenko, Dimitri A., Moore, Geoffrey R. and Le Brun, Nick E. 
ORCID: https://orcid.org/0000-0001-9780-4061
(2017)
Tyr25, Tyr58 and Trp133 of Escherichia coli bacterioferritin transfer electrons between iron in the central cavity and the ferroxidase centre.
Metallomics, 9 (10).
pp. 1421-1428.
ISSN 1756-5901
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Abstract
Ferritins are 24meric proteins that overcome problems of toxicity, insolubility and poor bioavailability of iron in all types of cells by storing it in the form of a ferric mineral within their central cavities. In the bacterioferritin (BFR) from Escherichia coli iron mineralization kinetics have been shown to be dependent on an intra-subunit catalytic diiron cofactor site (the ferroxidase centre), three closely located aromatic residues and an inner surface iron site. One of the aromatic residues, Tyr25, is the site of formation of a transient radical, but the roles of the other two residues, Tyr58 and Trp133, are unknown. Here we show that these residues are important for the rates of formation and decay of the Tyr25 radical and decay of a secondary radical observed during Tyr25 radical decay. The data support a mechanism in which these aromatic residues function in electron transfer from the inner surface site to the ferroxidase centre.
| Item Type: | Article |
|---|---|
| Faculty \ School: | Faculty of Science > School of Chemistry |
| UEA Research Groups: | Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017) Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry Faculty of Science > Research Groups > Chemistry of Life Processes Faculty of Science > Research Groups > Centre for Ocean and Atmospheric Sciences |
| Related URLs: | |
| Depositing User: | Pure Connector |
| Date Deposited: | 14 Sep 2017 05:05 |
| Last Modified: | 21 Oct 2022 16:30 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/64871 |
| DOI: | 10.1039/C7MT00187H |
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