University of Illinois Urbana-Champaign

Infrared studies of rhodopsin and its low temperature photoproducts, bathorhodopsin and isorhodopsin

Bagley, Kimberly Ann

This item is only available for download by members of the University of Illinois community. Students, faculty, and staff at the U of I may log in with your NetID and password to view the item. If you are trying to access an Illinois-restricted dissertation or thesis, you can request a copy through your library's Inter-Library Loan office or purchase a copy directly from ProQuest.

Permalink

https://hdl.handle.net/2142/25211

Description

Title
Infrared studies of rhodopsin and its low temperature photoproducts, bathorhodopsin and isorhodopsin
Author(s)
Bagley, Kimberly Ann
Issue Date
1987
Doctoral Committee Chair(s)
Frauenfelder, Hans
Department of Study
Physics
Discipline
Physics
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
  • Fourier-transform infrared difference spectroscopy
  • vebrational modes
  • chromophore
  • rhodopsin
  • bathorhodopsin
  • isorhodopsin
Language
en
Abstract
Fourier-transform infrared difference spectroscopy has been used to detect the vibrational modes of the chromophore and protein that change in position and intensity between rhodopsin and the photoproducts formed at low temperature (70K), bathorhodopsin and isorhodopsin. A method has been developed to obtain infrared difference spectra between rhodopsin and bathorhodopsin, bathorhodopsin and isorhodopsin, and rhodopsin and isorhodopsin. To aid in identification of the vibrational modes, experiments were performed on deuterated and hydrated films of native rod outer segments and rod outer segments regenerated with either retinal containing 13c at carbon-15 or 15-deuterioretinal, or hydrated films of rod outer segments regenerated with retinal containing 13c at either carbon-10, carbon-11, carbon-13, or carbons-14 and -15. These infrared studies provide independent verification of the resonance Raman result that the retinal in bathorhodopsin is all-trans-like. The positions of the C=N stretch in the deuterated pigment and the deuterated pigments regenerated with 11-cis 15-deuterioretinal or 11-cis retinal containing 13c at carbon-15 are indicative that the Schiff base linkage is protonated in rhodopsin, bathorhodopsin, and isorhodopsin. Furthermore, the C=N stretching frequency occurs at the same position in all three species. The data indicate that the protonated Schiff base has a C=N trans conformation in all three species, and that the ClO-Cll single bond is s-trans in bathorhodopsin. Finally, evidence is presented that, even in these early stages of the rhodopsin bleaching sequence, changes are occurring in the-opsin.
Type of Resource
text
Permalink
http://hdl.handle.net/2142/25211
Copyright and License Information
1987 Kimberly Ann Bagley

Owning Collections

Dissertations and Theses - Physics
Dissertations in Physics
Graduate Dissertations and Theses at Illinois PRIMARY
Graduate Theses and Dissertations at Illinois