Speaker
Description
Electron Transfer Flavoprotein (ETF) has been identified as a potential biochemical magnetoreceptor, modulating Reactive Oxygen Species (ROS) through a radical pair mechanism influenced by magnetic fields. This study integrates biophysical optimization frameworks from Part I with computational modeling to investigate ETF’s structural and functional responses to magnetic fields, particularly focusing on its β185 site. Using Marcus theory, electron transfer rates were calculated, correlating them with ROS modulation across both wild-type and mutant ETF structures, such as G267R. These calculations highlight the role of hyperfine interactions, Zeeman splitting, and triplet-singlet interconversion in facilitating ROS dynamics.
Molecular dynamics simulations identified key oxygen binding sites within ETF, linking specific structural features to ROS production. The β185 site was particularly responsive, with the G267R mutation showing hyperactive ROS generation due to altered electrostatic interactions. Optimized pulsed electromagnetic fields (PEMFs) resembling bang-bang control were applied to evaluate their impact on radical pair recombination and ROS modulation, revealing that tailored magnetic fields can significantly influence ETF activity.
This research provides a roadmap for leveraging magnetic field effects in oxidative stress management and metabolic disorders. The findings bridge theoretical constructs from Part I with biochemical specificity, illustrating how magnetic optimization frameworks can inform therapeutic strategies. By demonstrating the synergy between intrinsic protein dynamics and external magnetic fields, this study advances our understanding of ROS modulation and its potential applications in bioelectronic innovations and oxidative stress-related therapies.
