Paween Mahinthichaichan
Postdoctoral researcher
Address:
Beckman Institute, Room 3011,
University of Illinois at Urbana-Champaign,
405 N. Mathews Ave.,
Urbana, IL 61801.
E-mail:
Education
- B.S., Biochemistry
University of California, Riverside
- Ph.D., Biochemistry (Molecular Biophysics)
University of Illinois at Urbana-Champaign
Research Interests
- Molecular bioenergetics
- Enzymology
- Membrane channels
- Membrane biophysics
Publications
P. Mahinthichaichan*, D. M. Morris*, Y. Wang, G. Jensen*, and E. Tajkhorshid* (2018) Selective permeability of carboxysomes shell pores to anionic molecules.
J. Phys. Chem. B, in press
P.-C. Wen*, P. Mahinthichaichan*, N. Trebesch, T. Jiang, Z. Zhao, E. Shinn, Y. Wang, M. Shekhar, K. Kapoor, C. K. Chan, and E. Tajkhorshid (2018) Microscopic View of Lipids and Their Diverse Biological Functions.
Current Opinion in Structural Biology, 51: 177-186
P. Mahinthichaichan, R. B. Gennis*, E. Tajkhorshid* (2018) Bacterial denitrifying nitric oxide reductases and aerobic respiratory terminal oxidases use similar delivery pathways for their molecular substrates. BBA - Bioenergetics, 1859: 712-724
P. Mahinthichaichan, R. B. Gennis*, E. Tajkhorshid* (2018) Cytochrome aa3 oxygen reductase utilizes the tunnel observed in the crystal structures to deliver O2 for catalysis. Biochemistry, 57(14): 2150-2161.
S. Hong, J. H. Leung, C. Sun, P. Mahinthichaichan, L. Schurig-Briccio, P. S. Padyatti and R. B. Gennis (2018) Coupling Hydride Transfer to Proton Pumping: the Swiveling Mechanism of Transhydrogenase. Mechanisms of Primary Energy Transduction in Biology. Editor Marten Wikstrom. Royal Society of Chemistry. 104-139.
P.S. Padayatti, J. H. Leung, P. Mahinthichaichan, E. Tajkhorshid, A. Ishchenko, V. Cherezov, M. Soltis, B. J. Jackson, C. D. Stout, R. B. Gennis, and Q. Zhang (2017) Critical role of water molecules in proton translocation by the membrane-bound transhydrogenase. Structure, 25(7): 1111-1119.e3.
P. Mahinthichaichan, R. Gennis*, and E. Tajkhorshid* (2016)
All the O2 consumed by Thermus thermophilus cytochrome ba3 is delivered to the active site through a long, open hydrophobic tunnel with entrances within the lipid bilayer.
Biochemistry, 55(8): 1265-1278.
J. Vermaas, N. Trebesch, C. G. Mayne, S. Thangapandian, M. Shekhar, P. Mahinthichaichan, J. L. Baylon, T. Jiang, Y. Wang, M. P. Muller, E. Shinn, Z. Zhao, P.-C. Wen, and E. Tajkhorshid (2016)
Microscopic Characterization of Membrane Transport Function by In Silico Modeling and Simulation.
In Gregory A. Voth, editor: Methods in Enzymology, Vol 578: Computational Approaches for Studying Enzyme Mechanism Part B, MIE, UK: Academic Press, 2016, pp. 373-428.
C. G. Mayne, M. J. Arcario, P. Mahinthichaichan, J. L. Baylon, J. V. Vermaas, L. Navidpour, P.-C. Wen, S. Thangapandian, and E. Tajkhorshid (2016)
The Cellular Membrane as a Mediator for Small Molecule Interaction with Membrane Proteins.
Biochimica et Biophysica Acta - Biomembranes, 1058(10), 2290-2304.
Y. Ahn, P. Mahinthichaichan, H. J. Lee, H. Ouyang, D. Kaluka, S.-R. Yeh, D. Arjona, D. L. Rousseau, E. Tajkhorshid, P. Ädelroth, and R. B. Gennis (2014)
Conformational coupling between the active site and residues within the KC-channel of the Vibrio cholerae cbb3-type oxygen reductase.
Proceedings of the National Academy of Sciences USA, 111: E4419-E4428.
G. Enkavi, J. Li, P. Mahinthichaichan, P.-C. Wen, Z. Huang, S. A. Shaikh, and E. Tajkhorshid (2013)
Simulation Studies of the Mechanism of Membrane Transporters.
In Editors: Luca Monticelli and Emppu Salonen, "Biomolecular Simulations - Methods and Protocols", Humana Press.
Methods in Molecular Biology, Vol. 924, Part 2, 361-405.
R. R. Geyer, R. Musa-Aziz, G. Enkavi, P. Mahinthichaichan, E. Tajkhorshid, and W. Boron (2013)
Movement of NH3 through the Human Urea Transporter B (UT-B): A New Gas Channel.
American Journal of Physiology - Renal Physiology, 304: F1447-F1457.
M. T. Mizwicki, C. M. Bula, P. Mahinthichaichan, H. L. Henry, S. Ishizuka, A. W. Norman (2009)
On the mechanism underlying (23S)-25-dehydro-1alpha(OH)-vitamin D3-26,23-lactone antagonism of hVDRwt gene activation and its switch to a superagonist.
J. Biol. Chem., 284:36292-36301.