Three aromatic residues are required for electron transfer during iron mineralization in bacterioferritin

Ferritins are iron storage proteins that overcome the problems of toxicity and poor bioavailability of iron by catalyzing iron oxidation and mineralization through the activity of a diiron ferroxidase site. Unlike in other ferritins, the oxidized di-Fe3+ site of Escherichia coli bacterioferritin (Ec...

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Main Authors: Bradley, JM, Svistunenko, DA, Lawson, TL, Hemmings, AM, Moore, GR, Le Brun, NE
Format: Journal article
Language:English
Published: Wiley 2015
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author Bradley, JM
Svistunenko, DA
Lawson, TL
Hemmings, AM
Moore, GR
Le Brun, NE
author_facet Bradley, JM
Svistunenko, DA
Lawson, TL
Hemmings, AM
Moore, GR
Le Brun, NE
author_sort Bradley, JM
collection OXFORD
description Ferritins are iron storage proteins that overcome the problems of toxicity and poor bioavailability of iron by catalyzing iron oxidation and mineralization through the activity of a diiron ferroxidase site. Unlike in other ferritins, the oxidized di-Fe3+ site of Escherichia coli bacterioferritin (EcBFR) is stable and therefore does not function as a conduit for the transfer of Fe3+ into the storage cavity, but instead acts as a true catalytic cofactor that cycles its oxidation state while driving Fe2+ oxidation in the cavity. Herein, we demonstrate that EcBFR mineralization depends on three aromatic residues near the diiron site, Tyr25, Tyr58, and Trp133, and that a transient radical is formed on Tyr25. The data indicate that the aromatic residues, together with a previously identified inner surface iron site, promote mineralization by ensuring the simultaneous delivery of two electrons, derived from Fe2+ oxidation in the BFR cavity, to the di-ferric catalytic site for safe reduction of O2.
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spelling oxford-uuid:226462ad-661c-4f04-a27b-885ffa1a7ae42022-05-12T11:02:01ZThree aromatic residues are required for electron transfer during iron mineralization in bacterioferritinJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:226462ad-661c-4f04-a27b-885ffa1a7ae4EnglishSymplectic ElementsWiley2015Bradley, JMSvistunenko, DALawson, TLHemmings, AMMoore, GRLe Brun, NEFerritins are iron storage proteins that overcome the problems of toxicity and poor bioavailability of iron by catalyzing iron oxidation and mineralization through the activity of a diiron ferroxidase site. Unlike in other ferritins, the oxidized di-Fe3+ site of Escherichia coli bacterioferritin (EcBFR) is stable and therefore does not function as a conduit for the transfer of Fe3+ into the storage cavity, but instead acts as a true catalytic cofactor that cycles its oxidation state while driving Fe2+ oxidation in the cavity. Herein, we demonstrate that EcBFR mineralization depends on three aromatic residues near the diiron site, Tyr25, Tyr58, and Trp133, and that a transient radical is formed on Tyr25. The data indicate that the aromatic residues, together with a previously identified inner surface iron site, promote mineralization by ensuring the simultaneous delivery of two electrons, derived from Fe2+ oxidation in the BFR cavity, to the di-ferric catalytic site for safe reduction of O2.
spellingShingle Bradley, JM
Svistunenko, DA
Lawson, TL
Hemmings, AM
Moore, GR
Le Brun, NE
Three aromatic residues are required for electron transfer during iron mineralization in bacterioferritin
title Three aromatic residues are required for electron transfer during iron mineralization in bacterioferritin
title_full Three aromatic residues are required for electron transfer during iron mineralization in bacterioferritin
title_fullStr Three aromatic residues are required for electron transfer during iron mineralization in bacterioferritin
title_full_unstemmed Three aromatic residues are required for electron transfer during iron mineralization in bacterioferritin
title_short Three aromatic residues are required for electron transfer during iron mineralization in bacterioferritin
title_sort three aromatic residues are required for electron transfer during iron mineralization in bacterioferritin
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