Department of Chemistry and Biochemistry
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- Daniel W. Armstrong
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- Alejandro Bugarin
- Saiful Chowdhury
- Purnendu (Sandy) K. Dasgupta
- Rasika Dias
- Ronald L. Elsenbaumer
- Frank W. Foss
- Robert F. Francis
- Jongyun Heo
- Junha Jeon
- Kayunta Johnson-Winters
- Peter Kroll
- Carl J. Lovely
- Frederick MacDonnell
- Subhrangsu S. Mandal
- Dennis S. Marynick
- Roshan Perera
- Brad S. Pierce
- Martin Pomerantz
- Laszlo Prokai
- Krishnan Rajeshwar
- Jimmy R. Rogers
- Zoltan A. Schelly
- Kevin A. Schug
- E. Thomas Strom
- Norma Tacconi (Retired)
- Seiichiro Tanizaki
- Richard B. Timmons
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Office: 102 CRB, Email: email@example.com, Phone: 817-272-9067, FAX: 817-272-3808
# Chemical Biology # Proteins Containing Unnatural Amino Acids # Genetically Engineered Protein Therapeutics # Metalloenzymes in Physiological and Pathological Processes # Microarray Biochips # Solid-Phase Biochemical Synthesis and Biocatalysis
"Alkylamine-ligated H93G myoglobin cavity mutant: a model system for endogenous lysine and terminal amine ligation in heme proteins such as nitrite reductase and cytochrome f ", J. Du, R. Perera, J. H. Dawson. Inorg. Chem. 2011, 50 (4), 1242 - 1249.
"Molecular basis for the inability of an oxygen atom donor ligand to replace the natural sulfur donor heme axial ligand in cytochrome P450 catalysis. Spectroscopic characterization of the Cys436Ser CYP2B4 mutant", R. Perera, M. Sono, H. L. Voegtle, J. H. Dawson. Arch. Biochem. Biophys. 2011, 507 (1), 119 -125.
"Stabilization and spectroscopic characterization of the dioxygen complex of wild-type cytochrome P4502B4 (CYP2B4) and its distal side E301Q, T302A and proximal side F429H mutants at subzero temperatures", R. Perera, M. Sono, R. Kinloch, H. Zhang, M. Tarasev, S.C. Im, L. Waskell, J. H. Dawson Biochim. Biophys. Acta. 2011, 1814 (1), 69 - 75.
"Mechanistic studies of the immunochemical termination of self-tolerance with unnatural amino acids" J. Grünewald, G. S. Hunt, L. Dong, F. Niessen, B. G. Wen, M. L. Tsao, R. Perera, M. Kang, B. A. Laffitte, S. Azarian, W. Ruf, M. Nasoff, R. A. Lerner, P. G. Schultz, V. V. Smider. Proc. Natl. Acad. Sci. U. S. A. 2009, 106 (11), 4337 - 4342.
“Immunochemical Termination of Self-Tolerance,” J. Grünewald, M. L. Tsao, R. Perera, L. Dong, F. Niessen, B. G. Wen, D. M. Kubitz, V. V. Smider, W. Ruf, M. Nasoff, R. A. Lerner, P. G. Schultz. Proc. Natl. Acad. Sci. U.S.A. 2008, 105 (32), 11276-80.
“Selecting Folded Proteins from a Library of Secondary Structural Elements,” J. J. Graziano, W. Liu, R. Perera, B. H. Geierstanger, S. A. Lesley, P. G. Schultz. J. Am. Chem. Soc. 2008, 130 (1), 176-185.
“A Genetically Encoded Infrared Probe,” K. C. Schultz, L. Supekova, Y. Ryu, J. Xie, R. Perera*, P. G. Schultz*. J. Am. Chem. Soc. 2006, 128 (43), 13984-13985.
“Rapid Freeze-Quench ENDOR Study of Chloroperoxidase Compound I: The Site of the Radical”, S. H. Kim, R. Perera, L. P. Hager, J. H. Dawson, B. M. Hoffman. J. Am. Chem. Soc. 2006, 128 (17), 5598-5599.
“Structures of Thiolate- and Carboxylate-Ligated Ferric H93G Myoglobin: Models for Cytochrome P450 and for Oxyanion-Bound Heme Proteins”, R. Perera, J. Qin, L. L. Lovelace, J. H. Dawson, L. Lebioda. Biochemistry 2006, 45 (10), 3170-3177.
“Subzero-temperature Stabilization and Spectroscopic Characterization of Homogeneous Oxyferrous Complex of the Cytochrome P450 BM3 (CYP 102) Oxygenase Domain and Holoenzyme”, R. Perera, M. Sono, G. Raner, J. H. Dawson. Biochem. Biophys. Res. Commun. 2005, 338 (1), 365-371.
“The influence of substrate on the spectral properties of oxyferrous Wild-Type and T252A Cytochrome P450-CAM”, M. Sono, R. Perera, S. Jin, S. G. Sligar, T. A. Bryson, J. H. Dawson. Arch. Biochem. Biophys. 2005, 436, 40-49.
“Substrate Modulation of the Properties and Reactivity of the Oxy-Ferrous and Hydroperoxo-Ferric Intermediates of Cytochrome P450cam as Shown by Cryoreduction-EPR/ENDOR Spectroscopy”, R. Davydov, R. Perera, S. Jin, T. C. Yang, T. A. Bryson, M. Sono, J. H. Dawson, B. M. Hoffman. J. Am. Chem. Soc. 2005, 127 (5), 1403-1413.
“Cryoreduction EPR and 13C, 19F ENDOR Study of Substrate-Bound Substates and Solvent Kinetic Isotope Effect in the Catalytic Cycle of Cytochrome P450cam and its T252A Mutant”, S. H. Kim, T. Yang, R. Perera, S. Jin, T. A. Bryson, M. Sono, R. Davydov, J. H. Dawson, B. M. Hoffman. Dalton Trans. 2005, 21, 3464-3469.
“Modeling Heme Protein Active Sites with the His93Gly Cavity Mutant of Sperm Whale Myoglobin: Complexes with Nitrogen-, Oxygen- and Sulfur-Donor Proximal Ligands”, R. Perera, J. H. Dawson. J. Porphyrins Phthalocyanines, 2004, 8, 246-254.
“EpoK, a Cytochrome P450 Involved in Biosynthesis of the Potential Anticancer Drugs Epothilone A and B. Substrate-Mediated Rescue of a P450 Enzyme”, H. Ogura, C. R. Nishida, U. R. Hoch, R. Perera, J. H. Dawson, P. R. Ortiz de Montellano. Biochemistry 2004, 43, 14712-14721.
“Spectroscopic Characterization of Five- and Six-Coordinate Ferrous-NO Heme Complexes. Evidence for Heme Fe-Proximal Cysteinate Bond Cleavage in the Ferrous-NO Adducts of the Trp-409Tyr/Phe Proximal Environment Mutants of Neuronal NOS”, H. L. Voegtle, M. Sono, S. Adak, A. E. Pond, T. Tomita, R. Perera, D. B. Goodin, M. Ikeda-Saito, D. J. Stuehr, J. H. Dawson. Biochemistry 2003, 42 (8), 2475-2484.
“Neutral Thiol as a Proximal Ligand to Ferrous Heme Iron: Implications for Heme Proteins that Lose Cysteine Thiolate Ligation on Reduction,” R. Perera, M. Sono, J. A. Sigman, T. D. Pfister, Y. Lu, J. H. Dawson. Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 3641-3646.
“Cytochrome P450-Catalyzed Hydroxylations and Epoxidations”, Perera, R.; Jin, S.; Sono, M.; Dawson, J. H. in Metal Ions in Life Sciences, Volume 3: The Ubiquitous Roles of Cytochrome P450 Proteins; A. Sigel, H. Sigel, R. K. O. Sigel, Eds.; John Wiley & Sons Ltd., Chichester, UK; 2007; pp 319-354.
B.S. (Chemistry), Institute of Chemistry Ceylon (1997)
M.S. (Chemistry), University of Tromsø, Norway (1999)
Ph.D. (Biochemistry) University of South Carolina (2005)
Postdoctoral Research (Chemistry): The Scripps Research Institute (2005-2008)
Roshan Perera grew up on the outskirts of Colombo, the Sri Lankan capital. A Chemistry (Honors) graduate, he obtained a Master's degree in organic chemistry from the University of Tromsoe, Norway. During his Master’s he worked on Sharpless asymmetric dihydroxylation (AD) of olefins under the supervision of John S. Svendsen. He was also a Norwegian Government Scholar from 1997-1999 at the University of Tromsoe. From 1999 to 2000, he worked with David F. Bocian and Abhik Ghosh at the University of California-Riverside studying unsymmetrical porphyrin dimer complexes in bioinorganic chemistry. In 2005, he completed his Ph.D. in organic chemistry/biochemistry at the University of South Carolina under the tutelage of John H. Dawson. His dissertation work was on the structural and functional properties of cytochrome P450 and heme proteins. Here, Roshan also developed a novel approach to stabilize unstable oxyferrous complexes of metalloproteins. From 2005 to 2008, he was a postdoctoral fellow in Peter G. Schultz’s laboratory at The Scripps Research Institute (TSRI), where he researched proteins with genetically encoded unnatural amino acids to investigate their structure and function. He also worked extensively on the state-of-the-art technologies in chemistry, biology, automation, and information sciences at TSRI and the Genomics Institute of the Novartis Research Foundation (GNF). In 2008, he joined as an Assistant Professor in the Department of Chemistry at the University of Texas at Arlington (UTA). His research focus at UTA is the development of de novo approaches to understand complex scientific and biomedical problems using proteomics and genomics.
2008 College of Science Research Day - First Place Award, University of Texas, Arlington
2005 Graduate Research Symposium, Award for Excellence in Chemistry & Biochemistry, University of South Carolina
2005 Cancer Research Award, USC
2003 James R. Durig Graduate Student Award, USC
2000 Murtiashaw Fellowship in Organic Chemistry, USC
2000 Copenhaver Fellowship, USC
1997-1999 Norwegian Government Scholar, University of Tromsø-Norway