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 five
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.
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PqqE, a protein involved in PQQ biosynthesis, is a radical SAM enzyme. Biochemistry
Unique magnetic properties of 2-coordinate Fe(II) complexes. JACS
EasySpin can now simulate pulse EPR spectra. PCCP
High-field EPR of phycocyanobilin radical. JACS
Fluorotyrosine influences PCET events in PSII. JACS
New insights into MoFe cofactor biosynthesis. PNAS
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Congratulations to Stefan Stoll for his being awarded the International EPR Society's Young Investigator Award .
We have installed our cryogen free 0-8 Tesla sweepable magnet from Cryogenic Limited for our D-band spectrometer!
The Britt lab would like to welcome our new first-year physics student Emily Ricks.
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