Kinetics of iron release from pig spleen ferritin with bare platinum electrode reduction

Abstract

Several anaerobic electrochemical cells were employed to study the kinetics of iron release from pig spleen ferritin (PSF) at a bare platinum electrode. Controlled potential microcoulometry (CPM) is the principal technology used to investigate the kinetics in the absence of a mediator. A kinetic study of iron release by microcoulometry has revealed that ferritin undergoes direct electron transfer at the electrode in the absence of a mediator, indicating that ferritin is an electroactive protein. Several experiments failed to show that α′α-bipyridyl has the capacity to reduce hydrolyzed Fe 3+ within the ferritin core after it has been reduced by the electrode at −600 mV vs. NHE in the absence of mediator. PSF is known to bind heme to generate a hemeoprotein, named pig spleen hemeoferritin (PSF ho). The rate of iron release is accelerated by the heme binding to PSF ho without the need for small mediators. Under similar conditions, two kinetic processes for iron release from PSF and bacterial ferritin of Azoaobacter vinelandii (AvBF) were studied and both fit a zero-order law. In addition, the rate of iron release in PSF can be accelerated two-fold by a specific reduction system consisting of ascorbic acid (AA) and the bare platinum electrode at −600 mV. However, this kinetic process does not follow zero-, half-, first, or second-order rate laws. A model is proposed to explain a mechanism of direct electron transfer between ferritin and the electrode is derived to describe the kinetics of iron release.