Three Aromatic Residues are Required for Electron Transfer during Iron Mineralization in Bacterioferritin.

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 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

SUBMITTER: Bradley JM 

PROVIDER: S-EPMC4954121 | biostudies-literature | 2015 Dec

REPOSITORIES: biostudies-literature