2019 Bioinorganic Chemistry Award Winner


Professor R David Britt

Professor R David Britt

University of California, Davis

 

Awarded for developing state-of-the-art spectroscopic methods to characterize the active sites of metalloenzymes.

 


About the Winner


I studied physics at the BS and PhD levels.    For me, physics is most interesting as applied to understanding the interfaces to other major areas of science, so as a PhD student at Berkeley I chose to pursue research in experimental biophysics. Research into the light driven energy capture of photosynthesis seemed especially appealing, so I joined Melvin P. Klein's laboratory in the Melvin Calvin Laboratory for Chemical Biodynamics and focussed my research on spectroscopic studies of the Photosystem II manganese-containing oxygen evolving complex (OEC).   At that time the first EPR signals of intermediates of the S-state cycle were just appearing, and I decided to build a pulse EPR spectrometer in order to probe the OEC with much higher resolution than can be provided by conventional EPR.   We were able to show protein nitrogen coordination to the OEC and studied ammonia binding as a water oxidation inhibitor. Shortly after my PhD I moved to the Chemistry Dept at the University of California Davis, where I have spent my entire independent career.   My first students and I set out to build a more versatile lab-built pulse EPR instrument, which we used mostly to study the OEC in more detail, for example using pulse ENDOR.   As time when on we built or acquired a number of pulse and continuous wave instruments over an array of frequencies (8-263 GHz) and used them to study a wide variety of inorganic catalysts, metalloenzymes, and radical enzyme active sites. Systems relevant to sustainable energy have been forefront topics for us. The OEC and synthetic water oxidation catalysts remain high on our list of interesting spectroscopic targets.   With water split to harvest protons and electrons, hydrogen evolving catalysts can produce molecular hydrogen. This has led us toward recent studies of hydrogenase active sites, most notably the bio-assembly of the "H-cluster" of the Fe-Fe hydrogenase.


Related Links

Link icon R David Britt's webpage
University of California, Davis


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