Literature DB >> 6828860

Fourier transform infrared difference spectra of intermediates in rhodopsin bleaching.

K J Rothschild, W A Cantore, H Marrero.   

Abstract

The membrane protein rhodopsin is the primary light receptor in vision. Fourier transform infrared difference spectroscopy is sensitive to conformational changes in both the protein and the retinylidene chromophore of rhodopsin. By blocking rhodopsin bleaching at specific intermediates, it is possible to elucidate some of the primary molecular events of vision.

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Year:  1983        PMID： 6828860     DOI： 10.1126/science.6828860

Source DB:  PubMed          Journal:  Science        ISSN： 0036-8075            Impact factor:   47.728


  22 in total

Review 1.  FTIR difference spectroscopy of bacteriorhodopsin: toward a molecular model.

Authors:  K J Rothschild
Journal:  J Bioenerg Biomembr       Date:  1992-04       Impact factor: 2.945

2.  Structural comparison of metarhodopsin II, metarhodopsin III, and opsin based on kinetic analysis of Fourier transform infrared difference spectra.

Authors:  A L Klinger; M S Braiman
Journal:  Biophys J       Date:  1992-11       Impact factor: 4.033

3.  Local peptide movement in the photoreaction intermediate of rhodopsin.

Authors:  Hitoshi Nakamichi; Tetsuji Okada
Journal:  Proc Natl Acad Sci U S A       Date:  2006-08-14       Impact factor: 11.205

4.  Photoactivation of rhodopsin causes an increased hydrogen-deuterium exchange of buried peptide groups.

Authors:  P Rath; W J DeGrip; K J Rothschild
Journal:  Biophys J       Date:  1998-01       Impact factor: 4.033

5.  Two-photon spectroscopy of locked-11-cis-rhodopsin: evidence for a protonated Schiff base in a neutral protein binding site.

Authors:  R R Birge; L P Murray; B M Pierce; H Akita; V Balogh-Nair; L A Findsen; K Nakanishi
Journal:  Proc Natl Acad Sci U S A       Date:  1985-06       Impact factor: 11.205

6.  Incorporation of the nicotinic acetylcholine receptor into planar multilamellar films: characterization by fluorescence and Fourier transform infrared difference spectroscopy.

Authors:  J E Baenziger; K W Miller; K J Rothschild
Journal:  Biophys J       Date:  1992-04       Impact factor: 4.033

Review 7.  Synthetic retinals as probes for the binding site and photoreactions in rhodopsins.

Authors:  M Ottolenghi; M Sheves
Journal:  J Membr Biol       Date:  1989-12       Impact factor: 1.843

8.  The nature of the primary photochemical events in rhodopsin and isorhodopsin.

Authors:  R R Birge; C M Einterz; H M Knapp; L P Murray
Journal:  Biophys J       Date:  1988-03       Impact factor: 4.033

9.  Excited-state structure and isomerization dynamics of the retinal chromophore in rhodopsin from resonance Raman intensities.

Authors:  G R Loppnow; R A Mathies
Journal:  Biophys J       Date:  1988-07       Impact factor: 4.033

10.  Vibrational analysis of the all-trans retinal protonated Schiff base.

Authors:  S O Smith; A B Myers; R A Mathies; J A Pardoen; C Winkel; E M van den Berg; J Lugtenburg
Journal:  Biophys J       Date:  1985-05       Impact factor: 4.033
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