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Wong, Steve G., Abdulqadir, Raz, Le Brun, Nick E. 
ORCID: https://orcid.org/0000-0001-9780-4061, Moore, Geoffrey R. and Mauk, A. Grant
(2012)
Fe-haem bound to Escherichia colibacterioferritin accelerates iron core formation by an electron transfer mechanism.
Biochemical Journal, 444 (3).
pp. 553-560.
ISSN 0264-6021
Abstract
BFR (bacterioferritin) is an iron storage and detoxification protein that differs from other ferritins by its ability to bind haem cofactors. Haem bound to BFR is believed to be involved in iron release and was previously thought not to play a role in iron core formation. Investigation of the effect of bound haem on formation of the iron core has been enabled in the present work by development of a method for reconstitution of BFR from Escherichia coli with exogenously added haem at elevated temperature in the presence of a relatively high concentration of sodium chloride. Kinetic analysis of iron oxidation by E. coli BFR preparations containing various amounts of haem revealed that haem bound to BFR decreases the rate of iron oxidation at the dinuclear iron ferroxidase sites but increases the rate of iron core formation. Similar kinetic analysis of BFR reconstituted with cobalt-haem revealed that this haem derivative has no influence on the rate of iron core formation. These observations argue that haem bound to E. coli BFR accelerates iron core formation by an electron-transfer-based mechanism.
| 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 Groups > Centre for Ocean and Atmospheric Sciences Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry Faculty of Science > Research Groups > Chemistry of Life Processes |
| Depositing User: | Rachel Smith |
| Date Deposited: | 08 May 2013 08:48 |
| Last Modified: | 23 Oct 2022 00:29 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/40916 |
| DOI: | 10.1042/BJ20112200 |
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