Study of manganese binding to the ferroxidase centre of human H-type ferritin.

Study of manganese binding to the ferroxidase centre of human H-type ferritin.
J Inorg Biochem. 2018 Feb 09;182:103-112
Authors: Ardini M, Howes BD, Fiorillo A, Falvo E, Sottini S, Rovai D, Lantieri M, Ilari A, Gatteschi D, Spina G, Chiancone E, Stefanini S, Fittipaldi M
Abstract
Ferritins are ubiquitous and conserved proteins endowed with enzymatic ferroxidase activity, that oxidize Fe(II) ions at the dimetal ferroxidase centre to form a mineralized Fe(III) oxide core deposited within the apo-protein shell. Herein, the in vitro formation of a heterodimetal cofactor constituted by Fe and Mn ions has been investigated in human H ferritin (hHFt). Namely, Mn and Fe binding at the hHFt ferroxidase centre and its effects on Fe(II) oxidation have been investigated by UV-Vis ferroxidation kinetics, fluorimetric titrations, multifrequency EPR, and preliminary Mössbauer spectroscopy. Our results show that in hHFt, both Fe(II) and Mn(II) bind the ferroxidase centre forming a Fe-Mn cofactor. Moreover, molecular oxygen seems to favour Mn(II) binding and increases the ferroxidation activity of the Mn-loaded protein. The data suggest that Mn influences the Fe binding and the efficiency of the ferroxidation reaction. The higher efficiency of the Mn-Fe heterometallic centre may have a physiological relevance in specific cell types (i.e. glia cells), where the concentration of Mn is the same order of magnitude as iron.
PMID: 29454149 [PubMed...

Source: Journal of Inorganic Biochemistry - February 9, 2018 Category: Biochemistry Authors: Ardini M, Howes BD, Fiorillo A, Falvo E, Sottini S, Rovai D, Lantieri M, Ilari A, Gatteschi D, Spina G, Chiancone E, Stefanini S, Fittipaldi M Tags: J Inorg Biochem Source Type: research