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Ferroxidase activity of G4DFsc (top) and 3His-G4DFsc (bottom) indicated by the formation of a strong oxo-to-ferric charge transfer band near 360 nm. The saturation of this feature occurs much faster for G4DFsc than 3His-G4DFsc (see insets), but is more intense for 3His-G4DFsc (~4600 M-1 cm-1 per di-iron site) than G4DFsc (~2300 M−1 cm−1 per di-iron site). These molar absorptivity values are in range with those observed for natural oxo-bridged di-iron proteins.
