Ribbon diagram of recombinant Cytochrome ba₃ refined at 2.3 Angstroms. PDB 1XME.

Y. Chen et al. (2005) "A homologous expression system for obtaining engineered cytochrome ba₃ from Thermus thermophilus HB8" Prot. Expr. Pur., In Press
L. M. Hunsicker-Wang et al. (2005) "A novel cryoprotection scheme for enhancing diffraction of crystals from recombinant cytochrome ba₃ oxidase from Thermus thermophilus " Acta Cryst., D 43, In Press .

 

The Fee laboratory moved from the Division of Biology at UC San Diego to Department of Molecular Biology at The Scripps Research Institute on May 1, 2003. Here we share space and facilities and many common interests with Professors C. David Stout and David B. Goodin.

Currently there are three general areas of research:

[3Fe-4S] cluster for distortion analysis (unpublished).

• Physical chemical properties and mechanism of action of the cytochrome c oxidase from Thermus thermophilus, cytochrome ba₃. Our latest success with this system is the development of a homologous recombinant expression system for this enzyme, which permits us to prepare useful quantities of both wild-type and site-selected mutant forms of the enzyme. The ribbon diagram above is a crystal structure of the recombinant ba₃ enzyme.

 

• Characterization of the soluble, recombinant Thermus Rieske protein that is produced by E. coli cells. Here we have active collaborations with Dr. Judy Hirst of Oxford University and Dr. Eckard M¸nck of Carnegie Mellon University. Our latest successes in this area involve a complete thermodynamic characterization of the redox and ionization properties of the Rieske [2Fe-2S] cluster, a 1.3 Angstrom structure of the oxidized protein, and the discovery of a novel electronic form of the reduced cluster, which is, remarkably, stable at pH 14!

 

• Theoretical analysis of high-resolution structural information to understand the combined electron and proton binding properties of the [3Fe-4S] cluster in Azotobacter Ferredoxin I; the so-called redox Bohr effect. This project represents a many-pronged collaboration involving Drs. Louis Noodleman, Stout, Hirst, and M¸nck. The latest success with this project is the development of a geometrical analysis of [4Fe-4S] and [3Fe-4S] cluster structures that permit quantification of cluster distortion.

 

• Past projects have included extensive studies of Cu/Zn- and Fe/Mn-superoxide dismutases.

 

Publications are arranged by project.

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