R. David Britt
For Collaborators
Split Water: The Boat
Our Mission

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.


Research Highlights

HydG contains a unique [5Fe5S] cluster. PNAS

Putidaredoxin senses P450 oxidation state. JACS First catalytically relevant Mn(III,IV) dimer in biology. JACS Stepwise assembly of the H-Cluster in hydrogenase. Biochemistry Christmas comes early to the Britt lab. Our new Bruker E-500 spectrometer is here.
High-valent asymmetric MnCa cluster models the OEC PNAS MDTB-bound intermediate is detected in biotin synthase. JACS
Nitrogen hyperfine determines oxidation state of coordinating Mn ion in PSII Biochemistry
Paramagnetic intermediates found during water oxidation by cobalt JACS
Featured in Chemical & Engineering News Science & Technology Concentrates

Histidine coordination to [2Fe-2S] cluster in MitoNEET JACS

Magnetic parameters determined for both histidines bound to dinuclear Mn catalase JPCB

Ala344 is a ligand to Mn in the oxygen evolving complex JACS