The interaction of water molecules with purple membrane suspension using 2H double-quantum filter, 1H and 2H diffusion nuclear magnetic resonance.

作者: Limor Frish , Noga Friedman , Mordechai Sheves , Yoram Cohen

DOI: 10.1002/BIP.20099

关键词: DiffusionMembraneTrimerProton NMRPopulationAnalytical chemistryMoleculeChemistryNuclear magnetic resonanceBacteriorhodopsinProton

摘要: Bacteriorhodopsin is a membrane protein of the purple (PM) Halobacterium salinarum, which isolated as sheets highly organized two-dimensional hexagonal microcrystals and for water molecules play crucial role that affects its function proton pump. In this paper we used single- double-quantum (2)H NMR well (1)H diffusion to characterize interaction with PM in D(2)O suspensions. We found that, under influence strong magnetic field on concentrated sample (0.61 mM), affect entire population residual quadrupolar splitting (upsilon(q) approximately 5.5 Hz, 298 K, at 11.7 T) observed molecules. coupling, creation time maximal DQF signal was obtained (tau(max)), relative intensity spectrum samples (referred herein order parameters) are very sensitive temperature, dilution, chemical modifications PM. D(2)O, these parameters seem reflect organization Interestingly, have some efficiency trimer packing, concluded from apo-membrane behavior. The data dionized blue membrane, partially delipidated sample, detergent-treated show parameters, dependent, structural integrity addition, revealed heating inside or outside magnet has, after cooling, different effect characteristics difference samples, were heated cooled presence absence field, corroborates conclusions above indirect reflections both microscopic macroscopic samples. measurements showed least three distinct populations could be identified, based their coefficients. These correlate previously reported system.

参考文章(65)
Michel Roux, Michel Seigneuret, Jean Louis Rigaud, NMR study of the interaction of cations with purple membrane and of the purple-blue transition Biochemistry. ,vol. 27, pp. 7009- 7015 ,(1988) , 10.1021/BI00418A051
Dieter Oesterhelt, Walther Stoeckenius, Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane Methods in Enzymology. ,vol. 31, pp. 667- 678 ,(1974) , 10.1016/0076-6879(74)31072-5
Bertil Halle, Vladimir P. Denisov, Magnetic relaxation dispersion studies of biomolecular solutions. Methods in Enzymology. ,vol. 338, pp. 178- 201 ,(2001) , 10.1016/S0076-6879(02)38220-X
Heiko Patzelt, Anne S. Ulrich, Hermann Egbringhoff, Petra Düx, Jennifer Ashurst, Bernd Simon, Hartmut Oschkinat, Dieter Oesterhelt, Towards structural investigations on isotope labelled native bacteriorhodopsin in detergent micelles by solution-state NMR spectroscopy Journal of Biomolecular NMR. ,vol. 10, pp. 95- 106 ,(1997) , 10.1023/A:1018300215322
Hideki Kandori, Role of internal water molecules in bacteriorhodopsin Biochimica et Biophysica Acta (BBA) - Bioenergetics. ,vol. 1460, pp. 177- 191 ,(2000) , 10.1016/S0005-2728(00)00138-9
Gottfried Otting, NMR studies of water bound to biological molecules Progress in Nuclear Magnetic Resonance Spectroscopy. ,vol. 31, pp. 259- 285 ,(1997) , 10.1016/S0079-6565(97)00012-5
Y. Gat, M. Sheves, A mechanism for controlling the pKa of the retinal protonated Schiff base in retinal proteins. A study with model compounds Journal of the American Chemical Society. ,vol. 115, pp. 3772- 3773 ,(1993) , 10.1021/JA00062A052
M. Braiman, R. Mathies, Resonance Raman spectra of bacteriorhodopsin's primary photoproduct: evidence for a distorted 13-cis retinal chromophore. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 79, pp. 403- 407 ,(1982) , 10.1073/PNAS.79.2.403
P.K. Rogan, G. Zaccai, Hydration in purple membrane as a function of relative humidity Journal of Molecular Biology. ,vol. 145, pp. 281- 284 ,(1981) , 10.1016/0022-2836(81)90344-2