R. David Britt is the Winston Ko Chair and Distinguished Professor of Chemistry at the University of California, Davis. Prof. Britt uses electron paramagnetic resonance (EPR) spectroscopy to study metalloenzymes and enzymes containing organic radicals in their active sites.Britt is the recipient of multiple awards for his research, including the Bioinorganic Chemistry Award in 2019 and the Bruker Prize in 2015 from the Royal Society of Chemistry. He has received a Gold Medal from the International EPR Society (2014), and the Zavoisky Award from the Kazan Scientific Center of the Russian Academy of Sciences (2018).He is a Fellow of the American Association for the Advancement of Science and of the Royal Society of Chemistry.

• 1. Magnetic Resonance Characterization of Physiologically Important Metal Ion Binding Sites in the Prion and Related Proteins2. The catalytic role of metal-radical/protein-based radicals in heme enzymes3. Rigid Cu2+-based spin labels for the study of higher-order DNA G-quadruplex structures4. Orthogonal spin labeling and membrane proteins: increasing the information content and going towards in cell applications5. Spectroscopic investigation of mono- and di-Mn-containing centers in biochemistry with an emphasis on application of paramagnetic resonance techniques6. In Vivo pO2 Imaging of Tumors: Oxymetry with Very Low-Frequency Electron Paramagnetic Resonance, an Update7. EPR contributions to understanding molybdenum-containing enzymes8. EPR spectroscopy of Type I reaction centers9. Characterization of a substrate-derived radical in the NosN reaction during the biosynthesis of nosiheptide10. Functional solvent-protein interactions characterized by using spin probe EPR spectroscopy11. Integrative Ensemble Modelling of Proteins and their Complexes with Distance Distribution Restraints12. Site directed spin label probes of the mechanism of the cyanobacterial circadian clock13. Pulsed EPR spectroscopy as a tool to probe non-canonical electronic structures in artificial metalloenzymes14. Light-induced Pulsed Dipolar EPR Spectroscopy for distance and orientation analysis15. Recent Advances in Dynamic Nuclear Polarization16. Advances in Rapid Scan EPR Spectroscopy17. Controlling and exploiting intrinsic unpaired electrons in metalloproteins18. EPR advances in characterizing radical SAM Enzymology19. Overhauser high field DNP20. Experimental Guidelines for Trapping Paramagnetic Reaction Intermediates in Radical S-Adenosylmethionine Enzymes21. EPR Characterization of Synthetic Structural and Functional Analogs of Metalloenzyme Active Sites22. EPR spectroscopy on kinases

R. David Britt is the Winston Ko Chair and Distinguished Professor of Chemistry at the University of California, Davis. Prof. Britt uses electron paramagnetic resonance (EPR) spectroscopy to study metalloenzymes and enzymes containing organic radicals in their active sites.Britt is the recipient of multiple awards for his research, including the Bioinorganic Chemistry Award in 2019 and the Bruker Prize in 2015 from the Royal Society of Chemistry. He has received a Gold Medal from the International EPR Society (2014), and the Zavoisky Award from the Kazan Scientific Center of the Russian Academy of Sciences (2018).He is a Fellow of the American Association for the Advancement of Science and of the Royal Society of Chemistry.

• 1. Magnetic Resonance Characterization of Physiologically Important Metal Ion Binding Sites in the Prion and Related Proteins2. The catalytic role of metal-radical/protein-based radicals in heme enzymes3. Rigid Cu2+-based spin labels for the study of higher-order DNA G-quadruplex structures4. Orthogonal spin labeling and membrane proteins: increasing the information content and going towards in cell applications5. Spectroscopic investigation of mono- and di-Mn-containing centers in biochemistry with an emphasis on application of paramagnetic resonance techniques6. In Vivo pO2 Imaging of Tumors: Oxymetry with Very Low-Frequency Electron Paramagnetic Resonance, an Update7. EPR contributions to understanding molybdenum-containing enzymes8. EPR spectroscopy of Type I reaction centers9. Characterization of a substrate-derived radical in the NosN reaction during the biosynthesis of nosiheptide10. Functional solvent-protein interactions characterized by using spin probe EPR spectroscopy11. Integrative Ensemble Modelling of Proteins and their Complexes with Distance Distribution Restraints12. Site directed spin label probes of the mechanism of the cyanobacterial circadian clock13. Pulsed EPR spectroscopy as a tool to probe non-canonical electronic structures in artificial metalloenzymes14. Light-induced Pulsed Dipolar EPR Spectroscopy for distance and orientation analysis15. Recent Advances in Dynamic Nuclear Polarization16. Advances in Rapid Scan EPR Spectroscopy17. Controlling and exploiting intrinsic unpaired electrons in metalloproteins18. EPR advances in characterizing radical SAM Enzymology19. Overhauser high field DNP20. Experimental Guidelines for Trapping Paramagnetic Reaction Intermediates in Radical S-Adenosylmethionine Enzymes21. EPR Characterization of Synthetic Structural and Functional Analogs of Metalloenzyme Active Sites22. EPR spectroscopy on kinases