Effect of a magnetic field on the activity of superoxide dismutase studied at the enzyme level.

Regulation of reactive oxygen species is essential for maintaining cellular homeostasis, and superoxide dismutase (SOD) is a key antioxidant enzyme responsible for the removal of superoxide. In this study, the effect of a static magnetic field on SOD activity was analyzed at the molecular level using a purified enzyme-based reaction system. Superoxide was generated through the xanthine oxidase (XOD)-xanthine reaction, and the magnetic field effect was evaluated using optical methods. Both superoxide generation and SOD-mediated superoxide removal were facilitated by the magnetic field. To further understand the enhanced scavenging activity, SOD was immobilized on an Au electrode surface, and electrochemical analyses confirmed that the electron transfer characteristics between the Cu center in SOD and the electrode were altered under the magnetic field. These results present, for a single-enzyme-level system, that a magnetic field can be involved in the electron transfer behavior of antioxidant enzymes and the resulting catalytic activity, and provide fundamental insight into the interaction between magnetic fields and biological redox reactions.