R. David Britt

R. David Britt

Position Title
Winston Ko Chair and Distinguished Professor

3469 Chemistry Annex

The Britt lab is investigating structure and function of biologically significant enzymes with redox-active transition metal centers, clusters or organic radicals in their active site. The oxygen-evolving complex of photosystem II, the enzyme complex responsible for water oxidation in photosynthesis, is the major biological system currently under investigation. Our primary research tool is advanced electron paramagnetic resonance (EPR) spectroscopy. We operate the CalEPR center, home to six continuous-wave and pulse EPR instruments ranging in frequency from 9 to 130 GHz. CalEPR is the largest center of its kind on the West coast.

Education, Awards and Professional Highlights

  • Fellow of the Royal Society of Chemistry (2019)
  • Bioinorganic Chemistry Award, Royal Society of Chemistry (2019)
  • Winston Ko Chair in Science Leadership (2018)
  • Zavoisky Award, Kazan Scientific Center of the Russian Academy of Sciences (2018)
  • Royal Society of Chemistry Bruker Prize (2015)
  • Gold Medal, International EPR Society (2014)
  • Fellow, American Association for the Advancement of Science (AAAS) (2012)
  • Dreyfus Award (1989-1994) 
  • Appointed to UC Davis (1989)
  • M.A., Ph.D. University of California, Berkeley (1980)
  • B.S. North Carolina State University (1978)

Representative Publications

  • ESuess, D. L. M., I Burstel, L. De La Paz, J. M. Kuchenreuther, C. Pham, S. P. Cramer, J. R. Swartz, and R. D. Britt. Cysteine as a Ligand Platform in the Biosynthesis of the FeFe Hydrogenase H-cluster. Proc. Natl. Acad. Sci. U.S.A., 112:11455-11460 (2015).
  • Tao, L., T. A. Stich, C. N. Butterfield, C. A. Romano, T. G. Spiro, B. M. Tebo, W. H. Casey, and R. D. Britt. Mn(II) Binding and Subsequent Oxidation by the Multicopper Oxidase MnxG Investigated by Electron Paramagnetic Resonance Spectroscopy. J. Am. Chem. Soc. 137:10563-10575 (2015).
  • Chang, Y. G., S. Cohen, C. Phong, W. K. Meyers, Y. I. Kim, R. Tseng, J. Lin, L. Zhang, J. Boyd, R. D. Britt, M. Rust, S. S. Golden, and A. LiWang. A protein fold switch joins the circadian oscillator to clock output in cyanobacteria. Science 349:324-328 (2015).
  • Oyala, P. H., T. A. Stich, R. J. Debus, and R. D. Britt. Ammonia Binds to the Dangler Manganese of the Photosystem II Oxygen-Evolving Complex. J. Am. Chem. Soc. 137:8829-8837 (2015).
  • Gagnon, D. M., M. B. Brophy, S. E. J. Bowman, T. A. Stich, C. L. Drennan, R. D. Britt, and E. M. Nolan. Manganese Binding Properties of Human Calprotectin Under Conditions of High and Low Calcium. J. Am. Chem. Soc. 137:3004-3016 (2015).
  • Dinis, P., D. L. M. Suess , S. J. Fox , J. E. Harmer , R. C. Driesener, L. De La Paz , J. R. Swartz, J. W Essex , R D. Britt, and P. L. Roach. X-ray Crystallographic and EPR Spectroscopic Analysis of HydG, a Maturase in [FeFe]-Hydrogenase H-Cluster Assembly. Proc. Natl. Acad. Sci. U.S.A. 112:1362-1367 (2015).
  • CKuchenreuther, J. M., W. K. Myers, D. L. M. Suess, T. A. Stich, V. Pelmentschikov, S. A. Shiigi, S. P. Cramer, J. R. Swartz, R. D. Britt, and S. J. George. The HydG Enzyme Generates an Fe(CO)2(CN) Synthon in Assembly of the FeFe Hydrogenase H-Cluster. Science 343:424-427 (2014).