Heme proteins play an important role in many biological processes. Three types of heme proteins are under inves-tigation in my research. The first class includes proteins like heme-binding protein A which is important in heme sequestering in Haemophilus influenzae. The second class is catalase-peroxidases, in particular, Mycobacterium tuberculosis KatG which is necessary for the activation of the antitubercular drug isonazid against tuberculosis. The third class is heme-based sensor proteins which are responsible for monitoring the presence of small mole-cules (like O2, CO or NO) and initiating the appropriate response. Spectroscopic techniques, like resonance Raman, UV-visible absorbance and electron spin resonance, along with reaction kinetics, followed by transient absorbance, are used to probe the structure function relationships in these various heme proteins.
G. S. Lukat-Rodgers, N. L. Wengenack, F. Rusnak and K. R. Rodgers, “Spectroscopic Comparison of the Heme Active Sites in WT KatG and its S315T Mutant,” Biochemistry 2000, in press (published on www).
G. S. Lukat-Rodgers, L. Tang and K. R. Rodgers, “Nitrosyl adducts of FixL as Probes of Heme Environment,” Journal of Biological Inorganic Chemistry 2000, in press. K. R. Rodgers, G. S. Lukat-Rodgers and L. Tang, “Spectroscopic Observation of a FixL Switching Intermediate,” J. Am. Chem. Soc. 1999, 121, 11241-11242.
G. S. Lukat-Rodgers, J. L. Rexine and K. R. Rodgers, “Heme Speciation in Alkaline Ferric FixL and Possible Tyrosine Involvement in the Signal Transduction Pathway for Regulation of Nitrogen Fixation.” Biochemistry 1998, 37, 13543-13552.
G. S. Lukat-Rodgers and K. R. Rodgers, “Characterization of Ferrous FixL Nitric Oxide Adducts by Resonance Raman Spectroscopy,” Biochemistry 1997, 36, 4178-4187.