ISSN 1000-6818CN 11-1892/O6CODEN WHXUEU
Acta Phys Chim Sin >> 0,Vol.>> Issue()>> 0-0     doi: 10.3866/PKU.WHXB201703061         中文摘要
Accepted manuscript
Fluorescence Dynamics of LicT Protein by Time-resolved Spectroscopy
CHANG Meng-Fang1, LI Lei1, CAO Xiao-Dan1, JIA Meng-Hui2, ZHOU Jia-Sheng1, CHEN Jin-Quan1, XU Jian-Hua1
1 State Key Laboratory of Precision Spectroscopy, East China Normal University, Shanghai 200062, P. R. China;
2 Chinese Academy of Sciences, Shanghai Institute of Optics and Fine Mechanics, Shanghai 201800, P. R. China
Full text: PDF (1178KB) Export: BibTeX | EndNote (RIS)

In this paper, the fluorescence dynamics of tryptophan residues in the LicT protein were determined by time-resolved fluorescence spectroscopy combined with UV absorption and steady-state fluorescence spectroscopy. Moreover, the local microenvironment and structural changes of LicT protein before and after activation were studied. The activated LicT protein, AC 141, prevents the transcriptional antitermination of genes involved in carbohydrate utilization, which accelerates the organism's metabolism. The structural properties and microenvironment of AC 141 and the wild-type protein, Q 22, were determined by differences in the wavelength/intensity of tryptophan-associated fluorescence emissions, as well as in the lifetimes of these emissions. The interaction between tryptophan residues and the solvent was elucidated by decay-associated spectroscopy (DAS) and time-resolved emission spectra (TRES). These methods indicate that, upon activation, the structure of AC 141 is more compact than that of wild-type Q 22. In addition, TRES also showed that tryptophan residues in the protein had a continuous spectral relaxation process. Anisotropy experiments, which illustrate the conformational motions of amino acid residues and whole proteins, suggested that tryptophan residues had independent local motions in the protein system, and that the motions were more intense in the activated protein.

Keywords: Time-correlated single-photon counting   Tryptophan   Decay-associated spectra   Time-resolved emission spectra   Anisotropy  
Received: 2017-01-05 Accepted: 2017-03-01 Publication Date (Web): 2017-03-06
Corresponding Authors: XU Jian-Hua Email:

Cite this article: CHANG Meng-Fang, LI Lei, CAO Xiao-Dan, JIA Meng-Hui, ZHOU Jia-Sheng, CHEN Jin-Quan, XU Jian-Hua. Fluorescence Dynamics of LicT Protein by Time-resolved Spectroscopy[J]. Acta Phys. -Chim. Sin., 0, (): 0-0.    doi: 10.3866/PKU.WHXB201703061

(1) Frauenfelder, H.; Sligar, S. G.; Wolynes, P. G. Science 1991, 254 (5038), 1598. doi: 10.1126/science.1749933
(2) Xu, J.; Toptygin, D.; Graver, K. J.; Albertini, R. A.; Savtchenko, R.S.; Meadow, N. D.; Roseman, S.; Callis, P. R.; Brand, L.; Knutson, J. R. J. Am. Chem. Soc. 2006, 128 (4), 1214. doi: 10.1021/ja055746h
(3) Schimmel, P.; Cantor, C., Biophysical Chemistry: Part II;Techniques for the Study of Biological Structure and Function.New York: WH Freeman: 1980; pp:14-178.
(4) Lu, W.; Kim, J.; Qiu, W.; Zhong, D. Chem. Phys. Lett. 2004, 388 (1–3), 120. doi: 10.1016/j.cplett.2004.03.012
(5) Callis, P. R. Method. Enzymol. 1996, 278, 113. doi: 10.1016/S0076-6879(97)78009-1
(6) Longworth, J. W., Intrinsic Fluorescence of Proteins. InTime-Resolved Fluorescence Spectroscopy in Biochemistry andBiology, Cundall, R. B.; Dale, R. E., Eds. Springer US: Boston, MA, 1983; pp 651-725.
(7) Knutson, J. R.; Walbridge, D. G.; Brand, L. Biochemistry 1982, 21 (19), 4671. doi: 10.1021/bi00262a024
(8) McMahon, L. P.; Yu, H.-T.; Vela, M. A.; Morales, G. A.; Shui, L.; Fronczek, F. R.; McLaughlin, M. L.; Barkley, M. D. J. Phys. Chem.B 1997, 101 (16), 3269. doi: 10.1021/jp963273i
(9) Ross, J. B. A.; Wyssbrod, H. R.; Porter, R. A.; Schwartz, G. P.; Michaels, C. A.; Laws, W. R. Biochemistry 1992, 31 (6), 1585. doi: 10.1021/bi00121a002
(10) Szabo, A. G.; Rayner, D. M. J. Am. Chem. Soc. 1980, 102 (2), 554563. doi: 10.1021/ja00522a020
(11) Chen, Y.; Barkley, M. D. Biochemistry 1998, 37 (28), 9976. doi: 10.1021/bi980274n
(12) Lakowicz, J. R., Principles of Fluorescence Spectroscopy. SpringerScience & Business Media: 2006; pp 102-605.
(13) Vincent, M.; Deveer, A. M.; Haas, G. H.; Verheij, H. M.; Gallay, J.Eur. J. Biochem. 1993, 215 (3), 531. doi: 10.1111/j.1432-1033.1993.tb18062.x
(14) Ross, J. B. A.; Schmidt, C. J.; Brand, L. Biochemistry 1981, 20 (15), 4369. doi: 10.1021/bi00518a021
(15) Deutscher, J.; Francke, C.; Postma, P. W. Microbiol. Mol. Biol. R.2006, 70 (4), 939. doi: 10.1128/MMBR.00024-06
(16) Stülke, J.; Arnaud, M.; Rapoport, G.; Martin-Verstraete, I. Mol.Microbiol. 1998, 28 (5), 865. doi: 10.1046/j.1365-2958.1998.00839.x
(17) van Tilbeurgh, H.; Le Coq, D.; Declerck, N. EMBO J. 2001, 20 (14), 3789. doi: 10.1093/emboj/20.14.3789
(18) Declerck, N.; Dutartre, H.; Receveur, V.; Dubois, V.; Royer, C.; Aymerich, S.; van Tilbeurgh, H. J. Mol. Biol. 2001, 314, 671. doi: 10.1006/jmbi.2001.5185
(19) Declerck, N.; Vincent, F.; Hoh, F.; Aymerich, S.; van Tilbeurgh, H.J. Mol. Biol. 1999, 294 (2), 389. doi: 10.1006/jmbi.1999.3256
(20) Gooch, J. W., Beer-Bouguer Law (Beer-Lambert Law). InEncyclopedic Dictionary of Polymers, Gooch, J. W., Ed. SpringerNew York: New York, NY, 2011; pp 72-72.
(21) Zhang, L.; Kao, Y.-T.; Qiu, W.; Wang, L.; Zhong, D. J. Phys. Chem.B 2006, 110 (37), 18097. doi: 10.1021/jp063025e
(22) Callis, P. R.; Burgess, B. K. J. Phys. Chem. B 1997, 101 (46), 9429. doi: 10.1021/jp972436f
(23) Pierce, D. W.; Boxer, S. G. Biophys. J. 1995, 68 (4), 1583. doi: 10.1016/S0006-3495(95)80331-0
(24) Qiu, W.; Li, T.; Zhang, L.; Yang, Y.; Kao, Y.-T.; Wang, L.; Zhong, D. Chem. Phys. 2008, 350 (1–3), 154. doi: 10.1016/j.chemphys.2008.01.061
(25) Gryczynski, I.; Wiczk, W.; Johnson, M. L.; Lakowicz, J. R.Biophys. Chem. 1988, 32 (2), 173. doi: 10.1016/0301-4622(88)87005-4
(26) Chen, R. F.; Knutson, J. R.; Ziffer, H.; Porter, D. Biochemistry 1991, 30 (21), 5184. doi: 10.1021/bi00235a011

1. LU Yang.Recent Progress in Crystal Facet Effect of TiO2 Photocatalysts[J]. Acta Phys. -Chim. Sin., 2016,32(9): 2185-2196
2. WANG Jing-Dong, LI Shuang, Lü Rong, YU An-Chi.Fluorescence Quenching of Eosin Y by Tyrosine[J]. Acta Phys. -Chim. Sin., 2015,31(9): 1787-1794
3. TANG Rui-Zhi, LI Hai-Xia, LIU Yan-Cheng, ZHANG Peng, CAO Xi-Yan, WANG Wen-Feng.Laser Flash Photolysis Study on Electron Transfer Oxidation Reaction of Tryptophan or Tyrosine with Triplet State Vitamin K3[J]. Acta Phys. -Chim. Sin., 2012,28(01): 213-216
4. PU Peng, XU Can, XIE Shu-Yu.Influence of the Size Effect on the Chemical Shielding Tensors of SiO2 Nanotubes[J]. Acta Phys. -Chim. Sin., 2011,27(09): 2227-2232
5. CHENG Xiang-Long;WU Ai-Hua;SHEN Xing-Hai;HE Yong-Ke.The Formation of Cyclodextrin Nanotube Induced by POPOP Molecule[J]. Acta Phys. -Chim. Sin., 2006,22(12): 1466-1472
6. WANG Hai-Long;WANG Xiu-Xi;WANG Yu;LIANG Hai-Yi .Molecular Dynamics Simulations of Low Index Surfaces Melting Behaviors for Metal Cu[J]. Acta Phys. -Chim. Sin., 2006,22(11): 1367-1371
7. LI Yong-Qing;LI Jian;SONG Peng;MA Feng-Cai.The Differential Interference Angle of Λ-Related Quantum Interference of 1Π-state Diatom[J]. Acta Phys. -Chim. Sin., 2006,22(05): 602-607
8. LI Hua; XU Cai-ling; ZHAO Guang-yu; LI Hu-lin.Preparation and Magnetic Properties of Amorphous Co-Pt Alloy Nanowire Arrays[J]. Acta Phys. -Chim. Sin., 2005,21(06): 641-645
9. Qi Hang, Zhu Tao, Liu Zhong-Fan.Gold Nanorods Sol Prepared by Electrolysis[J]. Acta Phys. -Chim. Sin., 2000,16(10): 956-960
10. Jiang Ji-Sen, Gao Lian, Yang Xie-Long, Guo Jing-Kun.Preparation and Mössbauer Studies of α-Fe2O3 Nanoparticle[J]. Acta Phys. -Chim. Sin., 2000,16(04): 312-316
11. Liu Shou-Xin, Fang Yu, Hu Dao-Dao, Lv Hong-Wang.Complexation between Poly(methacrylic acid) and Cationically Modified Polyacrylamide[J]. Acta Phys. -Chim. Sin., 2000,16(03): 214-220
12. Han Kui,Xu Yong-Sheng,Ma Shi-Hong,Wang Guo-Yi,Luo Long-Gen,Lu Xing-Ze.Studies on Optical Nonlinear Anisotropy in Hemicyanine LB Multilayers[J]. Acta Phys. -Chim. Sin., 1996,12(07): 589-593
13. ZHOU Ting-Ting, SONG Hua-Jie, HUANG Feng-Lei.The Slip and Anisotropy of TATB Crystal under Shock Loading via Molecular Dynamics study[J]. Acta Phys. -Chim. Sin., 0,(): 0-0
Copyright © 2006-2016 Editorial office of Acta Physico-Chimica Sinica
Address: College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, P.R.China
Service Tel: +8610-62751724 Fax: +8610-62756388
^ Top