{"id":727,"date":"2026-04-15T13:22:40","date_gmt":"2026-04-15T13:22:40","guid":{"rendered":"https:\/\/citations.tools.bio-logic.fr\/?p=727"},"modified":"2026-04-15T13:22:40","modified_gmt":"2026-04-15T13:22:40","slug":"%ce%bc-12-peroxobridged-di-ironiii-dimer-formation-in-human-h-chain-ferritin","status":"publish","type":"post","link":"https:\/\/citations.tools.bio-logic.fr\/?p=727","title":{"rendered":"\u03bc-1,2-Peroxobridged di-iron(III) dimer formation in human H-chain ferritin"},"content":{"rendered":"<h4>DOI:<\/h4>\n<p><a href=\"https:\/\/doi.org\/10.1042\/bj3640057\" target=\"_blank\" rel=\"noopener\">10.1042\/bj3640057<\/a><\/p>\n<h4>Authors:<\/h4>\n<p>Fadi Bou\u2010Abdallah, Georgia C. Papaefthymiou, Danielle M Scheswohl, Sean D. STANGA, Paolo Arosio, N. Dennis Chasteen<\/p>\n<h4>Abstract:<\/h4>\n<p>Biomineralization of the ferritin iron core involves a complex series of events in which H(2)O(2) is produced during iron oxidation by O(2) at a dinuclear centre, the &lsquo;ferroxidase site&rsquo;, located on the H-subunit of mammalian proteins. Rapid-freeze quench M\u00f6ssbauer spectroscopy was used to probe the early events of iron oxidation and mineralization in recombinant human ferritin containing 24 H-subunits. The spectra reveal that a mu-1,2-peroxodiFe(III) intermediate (species P) with M\u00f6ssbauer parameters delta (isomer shift)=0.58 mm\/s and DeltaE(Q) (quadrupole splitting)=1.07 mm\/s at 4.2 K is formed within 50 ms of mixing Fe(II) with the apoprotein. This intermediate accounts for almost all of the iron in the sample at 160 ms. It subsequently decays within 10 s to form a mu-oxodiFe(III)-protein complex (species D), which partially vacates the ferroxidase sites of the protein to generate Fe(III) clusters (species C) at a reaction time of 10 min. The intermediate peroxodiFe(III) complex does not decay under O(2)-limiting conditions, an observation suggesting inhibition of decay by unreacted Fe(II), or a possible role for O(2) in ferritin biomineralization in addition to that of direct oxidation of iron(II).<\/p>\n","protected":false},"excerpt":{"rendered":"<p>DOI: 10.1042\/bj3640057 Authors: Fadi Bou\u2010Abdallah, Georgia C. Papaefthymiou, Danielle M Scheswohl, Sean D. STANGA, Paolo Arosio, N. Dennis Chasteen Abstract: Biomineralization of the ferritin iron core involves a complex series of events in which H(2)O(2) is produced during iron oxidation by O(2) at a dinuclear centre, the &lsquo;ferroxidase site&rsquo;, located on the H-subunit of mammalian [&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-727","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\/727","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=727"}],"version-history":[{"count":0,"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=\/wp\/v2\/posts\/727\/revisions"}],"wp:attachment":[{"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=727"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=%2Fwp%2Fv2%2Fcategories&post=727"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/citations.tools.bio-logic.fr\/index.php?rest_route=%2Fwp%2Fv2%2Ftags&post=727"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}