SpectrofIuorimetric study on the weak interaction between ATP and Na-4-tosyl-L-arginine methyl ester hydrochloride

被引:7
作者
Ma, Yan-Qing [1 ]
Lue, Gong-Xuan
Li, Ying
Liu, Shu-Hua
Xian, Liang
机构
[1] Chinese Acad Sci, Lanzhou Inst Chem Phys, State Key Lab Oxo Synthesis & Select Oxidat, Lanzhou 730000, Peoples R China
[2] Grad Univ Chinese Acad Sci, Beijing 100049, Peoples R China
[3] Lanzhou Univ, Dept Chem, Lanzhou 730000, Peoples R China
关键词
N-a-4-tosyl-L-arginine methyl ester hydrochloride; adenosine-5'-triphosphate (ATP); binding site; fluorescence quenching; Fourier transform infrared (FT-IR) spectra;
D O I
10.1002/cjoc.200790233
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
In this paper, some new results on the selective weak interaction between N-alpha-4-tosyl-L-arginine methyl ester hydrochloride (TAME) and adenosine-5'-triphosphate (ATP) have been reported. Fluorescence spectrophotometry and Fourier transform infrared (FT-IR) spectroscopy were used to investigate this kind of weak interaction. In fluorescence experiments, obvious fluorescence quenching phenomena were observed when TAME was added, Which indicated the weak interactions between TAME and ATP. It has been identified by fluorescence titration experiments that TAME exhibited high selectivity to ATP over ADP and AMP. FT-IR spectral results showed that an ATP-TAME adduct was formed. The experimental results indicated that the interaction sites were the guanidinium group of TAME main-chain and the gamma-phosphate group of ATP, and the interaction took place through hydrogen bonding and electrostatic force. In addition, the effects of metal ions on the weak interaction between ATP and TAME, or between ATP and analogues of L-arginine were studied.
引用
收藏
页码:1253 / 1258
页数:6
相关论文
共 31 条
[1]   STRUCTURE AT 2.8-ANGSTROM RESOLUTION OF F1-ATPASE FROM BOVINE HEART-MITOCHONDRIA [J].
ABRAHAMS, JP ;
LESLIE, AGW ;
LUTTER, R ;
WALKER, JE .
NATURE, 1994, 370 (6491) :621-628
[2]   Ras catalyzes CTP hydrolysis by shifting negative charges from γ- to β-phosphate as revealed by time-resolved FTIR difference spectroscopy [J].
Allin, C ;
Gerwert, K .
BIOCHEMISTRY, 2001, 40 (10) :3037-3046
[3]   Modification of the intrinsic fluorescence and the biochemical behavior of ATP after irradiation with visible and near-infrared laser light [J].
Amat, A ;
Rigau, J ;
Waynant, RW ;
Ilev, IK ;
Tomas, J ;
Anders, JJ .
JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY, 2005, 81 (01) :26-32
[4]   A PERSPECTIVE OF THE BINDING CHANGE MECHANISM FOR ATP SYNTHESIS [J].
BOYER, PD .
FASEB JOURNAL, 1989, 3 (10) :2164-2178
[5]   THE BINDING CHANGE MECHANISM FOR ATP SYNTHASE - SOME PROBABILITIES AND POSSIBILITIES [J].
BOYER, PD .
BIOCHIMICA ET BIOPHYSICA ACTA, 1993, 1140 (03) :215-250
[6]   SOLID-STATE VIBRATIONAL-SPECTRA OF CALCIUM PYROPHOSPHATE DIHYDRATE [J].
CORNILSEN, BC .
JOURNAL OF MOLECULAR STRUCTURE, 1984, 117 (1-2) :1-9
[7]  
DONG Q, 1977, METHODS INFRARED SPE, P200
[8]   CHIRAL RECOGNITION OF AROMATIC CARBOXYLATE ANIONS BY AN OPTICALLY-ACTIVE ABIOTIC RECEPTOR CONTAINING A RIGID GUANIDINIUM BINDING SUBUNIT [J].
ECHAVARREN, A ;
GALAN, A ;
LEHN, JM ;
DEMENDOZA, J .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1989, 111 (13) :4994-4995
[9]   Differences in nucleotide-binding site of isoapyrases deduced from tryptophan fluorescence [J].
Espinosa, V ;
Kettlun, AM ;
Zanocco, A ;
Cardemil, E ;
Valenzuela, MA .
PHYTOCHEMISTRY, 2003, 63 (01) :7-14
[10]   Diprotected triflylguanidines: A new class of guanidinylation reagents [J].
Feichtinger, K ;
Zapf, C ;
Sings, HL ;
Goodman, M .
JOURNAL OF ORGANIC CHEMISTRY, 1998, 63 (12) :3804-3805