Structural changes in bacteriorhodopsin during the photocycle measured by time-resolved polarized fourier transform infrared spectroscopy

Biophysical Journal

Volumn 81, Issue 6, 2001, Pages 3577-3589

  Kelemen, L ^a   Ormos, P ^a  

^a INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE; BACTERIORHODOPSIN; SCHIFF BASE;

ARTICLE; INFRARED SPECTROSCOPY; MOTION; PROTEIN CONFORMATION; PROTEIN STRUCTURE; PROTON TRANSPORT; VIBRATION; X RAY DIFFRACTION;

EID: 0035201902     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(01)75988-7     Document Type: Article

References (34)

1. Fourier transform infrared difference spectroscopy of bacteriorhodopsin and its photoproducts
2. Electro-optical measurements on aqueous suspension of purple membrane from Halobacterium Halobium
3. The quantum efficiency for the photochemical conversion of the purple membrane protein
4. Protein, lipid and water organization in bacteriorhodopsin crystals: A molecular view of the purple membrane at 1.9 Å resolution
5. 412 intermediate by photoselection
6. Restriction of motion of protein side chains during the photocycle of bacteriorhodopsin
7. Orientation of the bacteriorhodopsin chromophore probed by polarized Fourier transform infrared difference spectroscopy
8. Photoisomerization in bacteriorhodopsin studied by FTIR, linear dichroism and photoselection experiments combined with quantum chemical theoretical analysis
9. Structural investigation of bacteriorhodopsin and some of its photoproducts by polarized Fourier transform infrared spectroscopic methods-difference spectroscopy and photoselection
10. Simultaneous monitoring of light-induced changes in protein side-group protonation, chromophore isomerization, and backbone motion of bacteriorhodopsin by time-resolved Fourier-transform infrared spectroscopy
11. The quantum efficiency of the bacteriorhodopsin photocycle
12. Localization and orientation of functional water molecules in bacteriorhodopsin as revealed by polarized Fourier transform infrared spectroscopy
13. Proton transfer reactions across bacteriorhodopsin and along the membrane
14. Photoselection and transient linear dichroism with oriented immobilized purple membranes: Evidence for motions of the C(20)-methyl group of the chromophore towards the cytoplasmic side of the membrane
15. Polarized FTIR spectroscopy distinguishes peptide backbone changes in the M and N photointermediates of bacteriorhodopsin
16. Electric signals during the bacteriorhodopsin photocycle, determined over a wide pH range
17. Coupling photoisomerization of retinal to directional transport in bacteriorhodopsin
18. Structural changes in bacteriorhodopsin during ion transport at 2 Angstrom resolution
19. Orientation of the infrared transition moments for an α-helix
20. 412 intermediate in the bacteriorhodopsin photocycle
21. Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane
22. Infrared spectroscopic demonstration of a conformational change in bacteriorhodopsin involved in proton pumping
23. Infrared study of the L, M, and N intermediates of bacteriorhodopsin using the photoreaction of M
24. Fourier transform infrared study of the N intermediate of bacteriorhodopsin
25. Bacteriorhodopsin's intramolecular proton-release pathway consists of a hydrogen-bonded network
26. Polarized infrared spectroscopy of oriented purple membrane
27. Asp96 deprotonation and transmembrane α-helical structural changes in bacteriorhodopsin
28. Complete identification of C = O stretching vibrational bands of protonated aspartic acid residues in the difference infrared spectra of M and N intermediates versus bacteriorhodopsin
29. Protein changes associated with reprotonation of the Schiff-base in the photocycle of Asp96→Asn bacteriorhodopsin
30. Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin
31. Vibrational analysis of the all-trans retinal protonated Schiff-base
32. Thermodynamics and energy coupling in the bacteriorhodopsin photocycle
33. Time-resolved step-scan FT-IR investigations of the transition from KL to L in the bacteriorhodopsin photocycle: Identification of chromophore twists by assigning hydrogenout-of-plane (HOOP) bending vibrations
34. Interaction of the protonated Schiff-base with the peptide backbone of Valine 49 and the intervening water molecule in the N photointermediate of bacteriorhodopsin