Chemistry & Biochemistry
Email: warintra @ brandeis.edu
Dept. of Biochemistry, MS 009
415 South Street
Waltham, MA 02454, USA
Phone (Lab): (781) 736-2326
I received my Ph.D. in Chemistry from University of Kentucky in 2014 (research advisor: Prof. Anne-Frances Miller). My Ph.D. research projects include:
- Use of pre-steady- state and steady-state kinetics, kinetic isotope effect (primary and solvent KIE), numerical simulation and 2D NMR to understand the unusual broad substrate repertoire of nitroreductase.
- Integrated computational approach (QM/MM) to the analysis of 15 N and 13 C NMR in active site of flavodoxin.
- 19 F NMR study on substrate activation by tuning of pKas in flavin-dependent aromatic hydroxylases.
Pitsawong, W., Sucharitakul, J., Prongjit, M., Tan, T-C., Spadiut, O., Haltrich, D., Divne, C., and Chaiyen, P. (2010) A Conserved active-Site threonine is important for both sugar and flavin oxidation of pyranose 2-oxidase. J. Biol. Chem. 285, 9697- 705.
Tan, T-C., Pitsawong, W., Wongnate, T., Spadiut, O., Haltrich, D., Chaiyen, P., and Divne, C. (2010) H-bonding and positive charge at the N(5)/O(4) locus are critical for covalent flavin attachment in trametes pyranose 2-oxidase. J. Mol. Biol. 402, 578-594.
Tinikul, R.*, Pitsawong, W.*, Sucharitakul, J., Nijvipakul, S., Ballou, DP., and Chaiyen, P. (2013) The transfer of reduced flavin mononucleotide from LuxG oxidoreductase to luciferase occurs via free diffusion. Biochemistry 52, 6834-6843. (*Equal contribution)
Pitsawong, W., Hoben JP., and Miller, AF. (2014) Understanding and exploiting the broad substrate repertoire of nitroreductase via kinetic mechanism. J. Biol. Chem. 289, 15203-14.
Pitsawong, W., Haynes, CA, Koder, RL., Rodgers, DW., and Miller, AF. (2017) Distinct hydride transfers for different substrates in a promiscuous enzyme: nitroreductase Structure 25, 978-987.