Rosenstiel Basic Medical Sciences Research Center, 655
DegreesUniversity of Illinois, Ph.D.
University of Pittsburgh, B.Sc.
ExpertiseSelf-assembly of chemical and biological systems. Transient interactions in solution by NMR. NMR of soluble proteins. Protein stability and folding by NMR and mutagenesis. Structure and function of metal-containing enzymes and proteins.
ProfileCytochromes P450 are enzymes that catalyze the oxidation of a vast number of organic compounds in nature. In humans, the P450s are responsible for steroid hormone biosyntheses, drug metabolism and a variety of other important metabolic roles. We are interested in understanding how these enzymes select for a particular substrate and then direct the oxidation to a specific site on the substrate molecule. Although nuclear magnetic resonance (NMR) is our primary research tool, we employ a wide variety of techniques (site-directed mutagenesis, enzyme activity assays, organic synthesis) to improve our understanding of these important enzymes. Webpage
|BCBP||297b||Master's Lab Research II|
|CHEM||11a||General Chemistry I|
|CHEM||15a||Honors General Chemistry I|
|CHEM||59b||Advanced Laboratory: Physical Chemistry|
|CHEM||146b||Advanced NMR Spectroscopy|
|CHEM||240b||Physical Chemistry Seminar|
|CHEM||250b||Biophysical Chemistry Seminar|
|CHEM||260b||Materials Chemistry Seminar|
Awards and Honors
Chair, special study section, National Institutes of Health (2014)
Invited commentary in the Proceedings of the National Academy of Sciences USA (2014)
Guest Editor, Proceedings of the National Academy of Sciences of the United States of America (2013)
Invited speaker, International Symposium on Cytochromes P450, University of Seattle (2013)
Invited Speaker, Symposium on Magnetic Resonance in Metalloproteins, ACS National Meeting, Anaheim, CA, March 25th-31st, 2011. (2011)
Invited Conferee, Symposium Toward a Strategic Vision for Basic Sciences for Chemical and Biological Defense (Defense Threat Reduction Agency, US Dept. of Defense), Georgia Institute of Technology. (2008)
Michael J. Fox Foundation Rapid Response Grant for "Structural mapping and drug design for prevention and treatment of Parkinson's disease." (2008)
Chair, Natl. Institutes of Health Study Section for High Field NMR Spectrometers (2007)
Expert Witness, High Court of Justice, Lundbeck v. Generics UK, London, UK. (2007)
Expert Witness, US Federal District Court, Forest Labs v. Ivax Pharmaceuticals Wilmington DE (2006)
Chair, NIH special study section for 900 MHz NMR spectrometers, February, 2003. (2003)
Member of NIH metallobiochemistry study section (1998 - 2002)
Johnson & Johnson grant "for continued research on complex molecular structures using NMR" (1994 - 1997)
Camille and Henry Dreyfus Teacher-Scholar Award (1993 - 1995)
Michael L. Walzer '56 Award for Teaching (1992)
National Science Foundation Young Investigator Award (1992 - 1997)
Fuson Award for Excellence in Organic Graduate Research (1985)
American Chemical Society Richard A. Glenn Award for Coal Chemistry (1981)
Y. Zhang, N. Zhou, J. Shi, S. Pochapsky, T. C. Pochapsky, B. Zhang, X. Zhang, and B. Xu. "Unfolding a molecular trefoil derived from a zwitterionic metallopeptide to form self-assembled nanostructures." Nature Communications in press. (2015). (forthcoming)
Pochapsky, Thomas Charles. "Examining how enzymes self-organize in a membrane." Proceedings of the National Academy of Sciences of the United States of America 111. (2014): 3659-3660 <www.pnas.org/cgi/doi/10.1073/pnas.1401325111>.
Pochapsky, Thomas Charles & Pochapsky, Susan Sondej. "NMR spectroscopy for characterizing structure and function of biomacromolecules." Molecular Biophysics for the Life Sciences. vol. 6 Ed. Norma Allewell & Ivan Raiment. New York: Springer, 2013. 113-173.
T. Gurry, O. Ullman, C. Fisher, I. Perovic, T. C. Pochapsky and C. Stultz. "The dynamic structure of alpha-synuclein multimers." Journal of the American Chemical Society 135. (2013): 3865-3872.
Asciutto, Eliana K., Young, Matthew J., Madura, Jeffry, Pochapsky, Susan Sondej, Pochapsky, Thomas C.. "Solution Structural Ensembles of Substrate-Free Cytochrome P450(cam)." Biochemistry 51. (2012): 3383-3393.
Li, Shengying, Tietz, Drew R., Rutaganira, Florentine U., Kells, Petrea M., Anzai, Yojiro ; Kato, F., Pochapsky, Thomas C., Sherman, David H., Podust, Larissa M.. "Substrate Recognition by the Multifunctional Cytochrome P450 MycG in Mycinamicin Hydroxylation and Epoxidation Reactions." J. Biol. Chem. 287. (2012): 37880-37890.
E. J. Friedman, H. X. Wang, K. Jiang, I. Perovic, A. Deshpande, T. C. Pochapsky, B. R. S. Temple, S. N. Hicks, T. K. Harden, and A. M. Jones. "Aci-reductone dioxygenase I (ARDI) is an effector of the heterotrimeric G protein beta subunit in Arabidopsis." J. Biol. Chem. 286. (2011): 30107-30118.
E. K. Asciutto, M. Dang, S. S. Pochapsky, J. Madura, and T. C. Pochapsky. "Experimentally restrained molecular dynamics simulations for characterizing the open states of cytochrome P450cam.." Biochemistry 50. (2011): 1664-1671.
M. Dang, S.S. Pochapsky and T. C. Pochapsky. "Spring-loading the active site of cytochrome P450cam." Metallomics 3. (2011): 339-343.
W. Wang, I. Perovic, J. Chittuluru, A. Kagnanovich, L. T. T. Nguyen, J. Liao, J. R. Auclair, D. Johnson, A. Landeru, A. K. Simorellis, S. Ju, M. R. Cookson, F. J. Asturias, J. N. Agar, B. N. Webb, C. H. Kang, D. Ringe, G. A. Petsko, T. C. Pochapsky and Q. "A soluble alpha-synuclein construct forms a dynamic tetramer." Proc. Natl. Acad. Sci. USA 108. (2011): 17797-17802.
R. Herbst, I. Perovic, V. Martin-Diaconescu, K. O'Brien, P. Chivers, S. Pochapsky, T. Pochapsky, and M. Maroney. "The communication between the zinc and nickel sites in dimeric HypA: Metal recognition and pH sensing." J. Am. Chem. Soc. 132. (2010): 10338-10351.
T. C. Pochapsky, S. Kazanis and M. Dang. "Conformational plasticity and structure/function relationships in cytochromes P450." Antioxidants and Redox Signalling 13. (2010): 1273-129
E. K. Asciutto, J. D. Madura, S. S. Pochapsky, B. OuYang, T. C. Pochapsky. "Structural and dynamic implications of an effector-induced backbone amide cis-trans isomerization in cytochrome P450cam." J. Mol. Biol. 388. 3 (2009): 916-923.
S. S. Pochapsky, M. Dang, B. OuYang, A. K. Simorellis and T. C. Pochapsky. "Redox-dependent dynamics in cytochrome P450cam." Biochemistry 48. (2009): 4254-4261.
Chai, S. C., Ju, T. T., Dang, M., Goldsmith, R. B., Maroney, M. J., Pochapsky, T. C.. "Characterization of metal binding in the active sites of acireductone dioxygenase isoforms from Klebsiella ATCC 8724." Biochemistry 47. 8 (2008): 2428-2438.
Hamuro, Yoshitomo, Molnar, Kathleen S., Coales, Stephen J., OuYang, Bo, Simorellis, Alana K., Pochapsky, Thomas C.. "Hydrogen-deuterium exchange mass spectrometry for investigation of backbone dynamics of oxidized and reduced cytochrome P450cam." Journal of Inorganic Biochemistry 102. 2 (2008): 364-370.
OuYang, Bo, Pochapsky, Susan Sondej, Dang, Marina, and Pochapsky, Thomas Charles. "A functional proline switch in cytochrome P450cam." Structure 16. 6 (2008): 916-923.
Pochapsky, S. S., Sunshine, J. C., Pochapsky, T. C.. "Completing the Circuit: Direct-Observe 13C,15N Double-Quantum Spectroscopy Permits Sequential Resonance Assignments near a Paramagnetic Center in Acireductone Dioxygenase." J. Am. Chem. Soc. 130. 7 (2008): 2156-2157.
T. C. Pochapsky, T. Ju, B. OuYang, M. Dang, R. Beaulieu, and G.M. Pagani. "Nickel in acireductone dioxygenase." "Nickel and Its Surprising Impact in Nature", Vol. 2 of 'Metal Ions in Life Sciences'. Ed. A. Sigel, H. Sigel, R. K. O. Sigel. Chichester, UK: John Wiley & Sons, Ltd., 2007. 473-500.
Thomas C. Pochapsky and Susan Sondej Pochapsky. NMR for Physical and Biological Scientists. 1st ed. New York: Taylor & Francis, Garland Science, 2007.
B. OuYang, S. S. Pochapsky, G. M. Pagani, and T. C. Pochapsky. "Specific effects of potassium ion binding on wild-type and L358P cytochrome P450cam." Biochemistry 45. (2006): 14379-14388.
Ju, T. T., Goldsmith, R. B., Chai, S. C., Maroney, M. J., Pochapsky, S. S., Pochapsky, T. C.. "One protein, two enzymes revisited: A structural entropy switch interconverts the two isoforms of acireductone dioxygenase." Journal of Molecular Biology 363. 4 (2006): 523-534.
L. Rui, S. S. Pochapsky & T. C. Pochapsky. "Comparison of the complexes formed by cytochrome P450cam with cytochrome b5 and putidaredoxin, two effectors of camphor hydroxylase activity." Biochemistry 45. (2006): 3887 ¿ 3897.
Pochapsky, T. C., Pochapsky, S. S., Ju, T. T., Hoefler, C., Liang, J.. "A refined model for the structure of acireductone dioxygenase from Klebsiella ATCC 8724 incorporating residual dipolar couplings." Journal Of Biomolecular NMR 34. 2 (2006): 117-127.
Sauter, M., Lorbiecke, R., OuYang, B., Pochapsky, T. C., Rzewuski, G.. "The immediate-early ethylene response gene OsARD1 encodes an acireductone dioxygenase involved in recycling of the ethylene precursor S-adenosylmethionine." Plant Journal 44. 5 (2005): 718-729.
Wei, J. Y., Pochapsky, T. C., Pochapsky, S. S.. "Detection of a high-barrier conformational change in the active site of cytochrome P450(cam) upon binding of putidaredoxin." Journal Of The American Chemical Society 127. 19 (2005): 6974-6976.
Pochapsky,Thomas Charles with M. Kostic. "1H, 13C and 15N chemical shift assignments of an enolase-phosphatase, E1 from Klebsiella oxtoca." J. Biomol. NMR 30. (2004): 359-360.
Pochapsky,Thomas Charles with Y. Zhang, M. Heinsen, M. Kostic, G. Pagani, L. Hedstrom, T. Riera, I. Perovic, B.B. Snider. "Analogs of 1-phospho-2,3-dioxo-5-methylthoiopentance, an acyclic intermediate in the methionine salvage pathway: a new preparation and characterization of activity with E1 enolase/phosphatase from Klebsieall oxytoca." Bioorganic and Medicinal Chemistry 12. (2004): 3847-3855.
Pochapsky,Thomas Charles with M. Kostic and R. Bernhardt. "A Conserved histidine in vertebrate type ferredoxins is critical for redox-dependent dynamics." Biochemistry 42. (2003): 8171-8182.
Pochapsky,Thomas Charles with S. S. Pochapsky and J. W. Wei. "A model for effector activity in a highly specific biological electron transfer complex: the cytochrome P450cam-putidaredoxin couple." Biochemistry 42. (2003): 5649-5656.