Time-resolved ultraviolet resonance Raman studies of protein structure: application to bacteriorhodopsin

Biochemistry ◽  
1992 ◽  
Vol 31 (23) ◽  
pp. 5328-5334 ◽  
Author(s):  
James B. Ames ◽  
Marianne Ros ◽  
Jan Raap ◽  
Johan Lugtenburg ◽  
Richard A. Mathies
1999 ◽  
Vol 19 (1-4) ◽  
pp. 165-168 ◽  
Author(s):  
Shoji Kaminaka ◽  
Richard A. Mathies

To obtain high quality time-resolved ultraviolet resonance Raman (UVRR) spectra of transient intermediates in the bacteriorhodopsin (BR) photocycle, we developed a new UVRR spectrometer. A home-made F=3.5 prism prefilter was used in front of a 50 cm CCD detected spectrograph to give high throughput, wide tunability, and excellent stray light rejection along with low dispersion. Using this system, we obtained 239.5 nm excited time-resolved UVRR spectra of BR which revealed small but significant features associated with the formation of the KL-intermediate at 10 ns delays. This difference spectrum exhibits intensity decreases at 1624, 1561, 1012 and 763cm-1 due to an altered environment of one or more Trp residues and a frequency shift of the Tyr ʋ8b band at 1602 cm-1. These signals show that the photoisomerization of retinal from all-trans to 13-cis induces significant changes in the structure and environment of aromatic residues that line the retinal binding pocket in only 10 ns.


2018 ◽  
Vol 103 ◽  
pp. 223-229 ◽  
Author(s):  
Ryan S. Jakubek ◽  
Joseph Handen ◽  
Stephen E. White ◽  
Sanford A. Asher ◽  
Igor K. Lednev

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