Study of manganese binding to the ferroxidase centre of human H-type ferritin
| Autor: | M. Lantieri, Emilia Chiancone, Silvia Sottini, Maria Fittipaldi, Annarita Fiorillo, Barry D. Howes, Gabriele Spina, Elisabetta Falvo, Donella Rovai, Simonetta Stefanini, Andrea Ilari, Dante Gatteschi, Matteo Ardini |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Human H ferritin Kinetics Ferroxidase activity Biochemistry Cofactor law.invention Inorganic Chemistry 03 medical and health sciences law Mössbauer spectroscopy Heterodimetal manganese-iron centre Humans Electron paramagnetic resonance Manganese biology Chemistry Electron Spin Resonance Spectroscopy Ceruloplasmin Ferroxidase centre EPR Mössbauer Apoferritins Protein Binding Ferritin Crystallography 030104 developmental biology biology.protein Titration |
| Zdroj: | Journal of inorganic biochemistry 182 (2018): 103–112. doi:10.1016/j.jinorgbio.2018.02.003 info:cnr-pdr/source/autori:Ardini M.; Howes B.D.; Fiorillo A.; Falvo E.; Sottini S.; Rovai D.; Lantieri M.; Ilari A.; Gatteschi D.; Spina G.; Chiancone E.; Stefanini S.; Fittipaldi M./titolo:Study of manganese binding to the ferroxidase centre of human H-type ferritin/doi:10.1016%2Fj.jinorgbio.2018.02.003/rivista:Journal of inorganic biochemistry/anno:2018/pagina_da:103/pagina_a:112/intervallo_pagine:103–112/volume:182 |
| ISSN: | 0162-0134 |
| Popis: | 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 Mossbauer 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. |
| Databáze: | OpenAIRE |
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