Effect of ELF e.m. fields on metalloprotein redox-active sites
| dc.creator | De Ninno, A. | |
| dc.creator | Prosdocimi, M. | |
| dc.creator | Ferrari, V. | |
| dc.creator | Gerardi, G. | |
| dc.creator | Barbaro, F. | |
| dc.creator | Badon, T. | |
| dc.creator | Bernardini, D. | |
| dc.date | 2008-01-18 | |
| dc.date.accessioned | 2026-07-07T08:55:21Z | |
| dc.date.available | 2026-07-07T08:55:21Z | |
| dc.description | The peculiarity of the distribution and geometry of metallic ions in enzymes pushed us to set the hypothesis that metallic ions in active-site act like tiny antennas able to pick up very feeble e.m. signals. Enzymatic activity of Cu2+, Zn2+ Superoxide Dismutase (SOD1) and Fe2+ Xanthine Oxidase (XO) has been studied, following in vitro generation and removal of free radicals. We observed that Superoxide radicals generation by XO is increased by a weak field having the Larmor frequency fL of Fe2+ while the SOD1 kinetics is sensibly reduced by exposure to a weak field having the frequency fL of Cu2+ ion. | |
| dc.description | 18 pages, 4 figures | |
| dc.identifier | https://arxiv.org/abs/0801.2920 | |
| dc.identifier | http://arxiv.org/abs/0801.2920 | |
| dc.identifier.uri | http://salesiana.dossiersoluciones.com/handle/123456789/146244 | |
| dc.subject | Biological Physics | |
| dc.subject | General Physics | |
| dc.title | Effect of ELF e.m. fields on metalloprotein redox-active sites | |
| dc.type | text |