{"id":528,"date":"2026-04-15T13:36:00","date_gmt":"2026-04-15T13:36:00","guid":{"rendered":"https:\/\/citations.tools.bio-logic.fr\/?p=528"},"modified":"2026-04-15T13:36:00","modified_gmt":"2026-04-15T13:36:00","slug":"three-aromatic-residues-are-required-for-electron-transfer-during-iron-mineralization-in-bacterioferritin","status":"publish","type":"post","link":"https:\/\/citations.tools.bio-logic.fr\/?p=528","title":{"rendered":"Three Aromatic Residues are Required for Electron Transfer during Iron Mineralization in Bacterioferritin"},"content":{"rendered":"<h4>DOI:<\/h4>\n<p><a href=\"https:\/\/doi.org\/10.1002\/anie.201507486\" target=\"_blank\" rel=\"noopener\">10.1002\/anie.201507486<\/a><\/p>\n<h4>Authors:<\/h4>\n<p>Justin M. Bradley, Dimitri A. Svistunenko, T. Lawson, Andrew M. Hemmings, Geoffrey R. Moore, Nick E. Le Brun<\/p>\n<h4>Abstract:<\/h4>\n<p>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-Fe(3+) site of Escherichia coli bacterioferritin (EcBFR) is stable and therefore does not function as a conduit for the transfer of Fe(3+) into the storage cavity, but instead acts as a true catalytic cofactor that cycles its oxidation state while driving Fe(2+) 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 Fe(2+) oxidation in the BFR cavity, to the di-ferric catalytic site for safe reduction of O2.<\/p>\n","protected":false},"excerpt":{"rendered":"<p>DOI: 10.1002\/anie.201507486 Authors: Justin M. Bradley, Dimitri A. Svistunenko, T. Lawson, Andrew M. Hemmings, Geoffrey R. Moore, Nick E. Le Brun Abstract: 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 [&hellip;]<\/p>\n","protected":false},"author":1,"featured_media":0,"comment_status":"open","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"footnotes":""},"categories":[5],"tags":[],"class_list":["post-528","post","type-post","status-publish","format-standard","hentry","category-freeze-quench"],"_links":{"self":[{"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=\/wp\/v2\/posts\/528","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=%2Fwp%2Fv2%2Fcomments&post=528"}],"version-history":[{"count":0,"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=\/wp\/v2\/posts\/528\/revisions"}],"wp:attachment":[{"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=528"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=%2Fwp%2Fv2%2Fcategories&post=528"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=%2Fwp%2Fv2%2Ftags&post=528"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}