Abstract
Peroxidase is one of the magnetosensitive enzymes, and has an important role in scavenging reactive oxygen species. In the present study, a surface of platinum black electrode was laminated by peroxidase molecules, and H2O2 decomposing processes by peroxidase and platinum black were monitored with and without magnetic fields of up to 14 T. An increase in the current reflected a decrease in the activity of peroxidase molecules. The current in the electrode with peroxidase increased significantly depending on the applied magnetic flux intensity. The increases of current during the magnetic field exposures were observed consistently both when the currents were transiently decreasing and at a constant level. It is suggested that the layers of peroxidase molecules on the platinum black cause a distortion by diamagnetic forces acting on the layers, and the distortion is concentrated on a catalytic part in the peroxidase resulting in the observed activity decreases.
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