Robert A. ScottProfessor of Chemistry and Biochemistry & Molecular Biology
Head, Department of Chemistry
Professor Scott received his B.S. from the University of Illinoisin 1975 and Ph.D. from the California Institute of Technology in 1980.He was an NIH Postdoctoral Fellow at Stanford University and an AssistantProfessor at the University of Illinois before joining the Georgia facultyin 1987. He received an NSF Presidential Young Investigator Award in 1985-1990.
Our group is involved in studying both structural (using X-ray absorption spectroscopy) and functional aspects of metal sites in biomolecules. We use molecular biology and biophysical tools to study the detailed effect of protein environment on metal-site characteristics. In particular, protein determinants of metal-site reduction potential, of heavy metal binding affinity, and of hyperthermostability are being investigated.
We are also involved in a biophysical and genetic study of the basal transcription system in P. furiosus. The single transcription systemin archaea appears to have been the ancestor of all three eukaryotic transcription systems. We have structurally characterized homologs of the eukaryotic TATA-binding protein (TBP, the promoter recognition element) and transcription factor (TF) IIB (that binds to TBP/promoter and recruits the RNA polymerase). We are examining protein-DNA binding and protein-protein interactions to define the molecular topography of the transcription pre-initiation complex in this archaeon.
Our long-standing involvment in X-ray absorption spectroscopy has recently turned to structural characterization of metalloprotein sites on a proteomic scale. High-throughput XAS techniques should allow us to characterize the "metalloproteome", the local metal-site structure for all expressed proteins from an organism under given growth conditions. Application of these techniques to metalloregulation and metal homeostasis is planned.
"Modulation of the Redox Potential of the Fe(SCys)4 Site in Rubredoxin by the Orientation of a Peptide Dipole," Eidsness, M. K.; Burden, A. E.; Richie, K. A.; Kurtz, Jr., D. M.; Scott, R. A.; Smith, E. T.; Ichiye, T.; Beard, B.; Min, T.; Kang, C. Biochemistry 1999, 38, 14803-14809.
"Structural Evidence for a Common Zinc Binding Domain in Archaeal and Eucaryal Transcription Factor IIB Proteins," Colangelo, C. M.; Lewis, L. M.; Cosper, N. J.; Scott, R. A. JBIC 2000, 5, 276-283.
"Structure of a (Cys3His) Zinc Ribbon, a Ubiquitous Motif in Archaeal and Eucaryal Transcription," Chen, H.-T.; Legault, P.; Glushka, J.; Omichinski, J. G.; Scott, R. A. Prot. Sci.2000, 9, 1743-1752.
"The Zinc Metalloregulatory Protein Synechococcus PCC7942 SmtB Binds a Single Zinc Ion per Monomer with High Affinity in a Tetrahedral Coordination Geometry," VanZile, M. L.; Cosper, N. J.; Scott, R. A.; Giedroc, D. P. Biochemistry2000, 39, 11818-11829.
"Direct Fe-S Cluster Involvement in Generation of a Radical in Lysine 2,3-Aminomutase," Cosper, N. J.; Booker, S. J.; Ruzicka, F.; Frey, P. A.; Scott, R. A. Biochemistry2000, 39, 15668-15673.
"Spectroscopic Properties of the Metalloregulatory Cd(II) and Pb(II) Sites of S. aureus pI258 CadC," Busenlehner, L. S.; Cosper, N. J.; Scott, R. A.; Rosen, B. P.; Giedroc, D. P. Biochemistry2001, 40, 4426-4436.
"Thermal stability of the [Fe(SCys)4] site in Clostridium pasteurianum rubredoxin: contributions of the local environment and Cys ligand protonation," Bonomi, F.; Burden, A. E.; Eidsness, M. K.; Fessas, D.; Iametti, S.; Kurtz Jr., D. M.; Mazzini, S.; Scott, R. A.; Zeng, Q. J. Biol. Inorg. Chem.2002, 7, 427-436.