Abstract
The red-ox reactions of the dinuclear iron center of mouse R2 protein upon interaction with different reductants (dithionite alone and with mediators) and oxidants (PES, methylene blue, hydrogen peroxide and para-benzoquinone) have been studied by EPR and optical spectroscopy. The obtained results indicate that the transitions between Fe(III)Fe(III), Fe(II)Fe(III), and Fe(II)Fe(II) states of the dinuclear iron center are reversible and the μ-oxo-bridge may be formed upon oxidation by non-oxygen oxidants. In contrast to the case for theE. coliR2 protein, dithionite alone reduces the tyrosyl radical and diiron center in mouse R2 protein.
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