Iron Oxidation in<i>Escherichia coli</i>Bacterioferritin Ferroxidase Centre, a Site Designed to React Rapidly with H<sub>2</sub>O<sub>2</sub>but Slowly with O<sub>2</sub>
نویسندگان
چکیده
Both O2 and H2O2 can oxidize iron at the ferroxidase center (FC) of Escherichia coli bacterioferritin (EcBfr) but mechanistic details two reactions need clarification. UV/Vis, EPR, Mössbauer spectroscopies have been used to follow when apo-EcBfr, pre-loaded anaerobically with Fe2+, was exposed or H2O2. We show that binds di-Fe2+ FC reversibly, Fe2+ ions are oxidized in concert a molecule is formed released solution. This peroxide further oxidizes another FC, rate circa 1000 faster than O2, ensuring an overall 1:4 stoichiometry oxidation by O2. Initially Fe3+ react (producing protein bound radicals) relaxes within seconds H2O2-unreactive di-Fe3+ form. The data obtained suggest primary role EcBfr vivo may be detoxify rather sequester iron.
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ژورنال
عنوان ژورنال: Angewandte Chemie
سال: 2021
ISSN: ['1521-3773', '1433-7851', '0570-0833']
DOI: https://doi.org/10.1002/anie.202015964