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Dr Gopal R Periyannan

Dr Gopal R Periyannan

Associate Professor - Biochemistry

Office: 4417 - Physical Science Bldg
Phone: 217-581-6379
Email: grperiyannan@eiu.edu
Website: http://www.ux1.eiu.edu/~grperiyannan/home.html

Frequently Taught Courses

CHM 1310 - General Chemistry I
CHM 1315 - General Chemistry I Laboratory
CHM 3300 - Survey of Biochemistry
CHM 3455 - Biochemistry Laboratory
CHM 3460 - Biochemistry III


B.Sc., University of Peradeniya (Sri Lanka), 1996
Ph.D., Miami University (Ohio), 2004
EIU, 2006

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Hydrolytic (Zn-metallo) enzymes


My research focuses on the structure and the mechanistic aspects of Zn-metalloenzymes in order to understand their physiological function and their role in disease development. One-third of all known enzymes are metalloenzymes. The number of important enzymes containing metal ions in their active site is increasing, which thereby underscores the significance of the role played by metalloenzymes in biology and medicine.

My research interest spans across several disciplines of biological chemistry, focusing on the following areas:

  • Zn-metalloenzymes.
  • Role of metalloproteases in cell signaling and cancer metastasis.
  • Prostate cancer and metalloproteases.
  • Zn-metalloproteases in the cell cycle of Schizosaccharomyces pombe and Caulobacter crescentus.
  • Spectroscopic characterization of metalloenzymes.
  • Bioinorganic chemistry.

Within my research, I use molecular biological/cloning techniques in bacterial and yeast expression systems to obtain the proteins of interest. Easy-to-handle eukaryotic model systems, such as fission and budding yeasts and functional genomic techniques, are employed to understand the functional significance of these metalloenzymes in eukaryotes.

A wide array of spectroscopic techniques, such as paramagnetic 1H NMR, EPR, UV-Vis, CD are used in my research. Spectroscopic and rapid kinetic techniques are also invaluable tools in the understanding of the chemical mechanism of metalloenzymes. For example, electron paramagnetic resonance (EPR) spectroscopy coupled with a freeze-quench facility or rapid scanning UV-Vis technique dramatically increases the possibility of observing reaction intermediates formed during the catalytic cycle of a metalloenzyme.

Selected Publications

A. L. Costello, G. R. Periyannan, K.-W. Yang, M. W. Crowder, D. L. Tierney, "Site selective binding of Zn(II) to metallo-ß-lactamase L1 from Stenotrophomonas maltophilia," JBIC 2006, 11(3), 351-8.

G. R. Periyannan, A. L. Costello, D. L. Tierney, K.-W. Yang, B. Bennett, M.W. Crowder, "Sequential binding of Co(II) to metallo-ß-lactamase CcrA," Biochemistry 2006, 45(4), 1313-1320.

G. P. K. Marasinghe, I. M. Sander, B. Bennett, G. R Periyannan, K.-W. Yang, C. A. Makaroff, M. W. Crowder, "Structural studies on a mitochondrial glyoxalase II," J. Biol. Chem. 2005, 280(49), 40668-40675.

G. R. Periyannan, P. Shaw, T. Sigdel, M. W. Crowder, “In vivo folding of recombinant metallo-ß-lactamase L1 requires the presence of Zn(II),” Protein Science 2004, 13, 2236-2243.

A. L. Carenbauer, J. D. Garrity, G. Periyannan, R. B. Yates, M. W. Crowder, “Probing substrate binding to metallo-β-lactamase L1 from Stenotrophomonas maltophilia by using site-directed mutagenesis,” BMC Biochem. 2002, 3(1), 4.

M. W. Crowder, K. -W. Yang, A. L. Carenbauer, G. Periyannan, M. E. Seifert, “The problem of solvent exposable disulfide when preparing Co(II)-substituted metallo-ß-lactamase L1 from Stenotrophomonas maltophilia,” JBIC 2001, 6, 91-99.

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