Abstract
Although Fe3O4 nanoparticles were early reported to outperform horseradish peroxidase (HRP), recent studies suggested that this material bears a very poor activity instead. Here, we resolve this disagreement by reviewing the definition of descriptors used and provide an atomic view into the origin of Fe3O4 nanoparticles as peroxidase mimetics. The redox between H2O2 and Fe(II) sites on the Fe3O4 surface was identified as the key step to producing OH radicals for the oxidation of colorimetric substrates. This mechanism involving free radicals is distinct from that of HRP oxidizing substrates with a radical retained on its Fe-porphyrin ring. Surprisingly, the distribution and chemical state of Fe species were found to be very different on single- and polycrystalline Fe3O4 nanoparticles with the latter bearing not only a higher Fe(II)/Fe(III) ratio but also a more reactive Fe(II) species at surface grain boundaries. This accounts for the unexpected gap in the catalytic constant (kcat) observed for this material in the literature.
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