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10.1002/anie.201507486

http://scihub22266oqcxt.onion/10.1002/anie.201507486
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suck abstract from ncbi


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pmid26474305      Angew+Chem+Int+Ed+Engl 2015 ; 54 (49): 14763-7
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  • Three Aromatic Residues are Required for Electron Transfer during Iron Mineralization in Bacterioferritin #MMPMID26474305
  • Bradley JM; Svistunenko DA; Lawson TL; Hemmings AM; Moore GR; Le Brun NE
  • Angew Chem Int Ed Engl 2015[Dec]; 54 (49): 14763-7 PMID26474305show ga
  • 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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