RESUMO
Under excitation by visible light the iron storage protein ferritin catalyses the reduction of cytochrome c and viologens as well as the oxidation of carboxylic acids, thiol compounds, and sulfite. The photochemically active element of ferritin is its mineral ferrihydrite semiconductor core. Band-gap excitation of these microcrystals leads to generation of electron-hole pairs that are sufficiently long-lived and reactive to engage in redox reactions with components of the medium. Photoreduction of cytochrome c and viologens occurs due to electron transfer from the conduction band of the iron oxide cluster through the protein shell surrounding the ferritin core. Laser photolysis coupled with time-resolved kinetics spectroscopy showed the electron transfer to propylviologen sulfonate to proceed in the microsecond time range. In the absence of electron acceptor at pH < 7, light excitation results in photodissolution of the iron oxide cluster with concomitant formation of Fe(II). These novel findings concerning the photocatalytic activity of ferritin with its inherent biological implications are discussed.
