Literature DB >> 427199

Resonance Raman study of the dark-adapted form of the purple membrane protein.

B Aton, A G Doukas, R H Callender, B Becher, T G Ebrey.   

Abstract

The resonance Raman spectrum of the dark-adapted form of the purple membrane protein (bacteriorhodopsin) has been obtained and is compared to the light-adapted pigment and model chromophore spectra. As in the light-adapted form, the chromophore-protein linkage is found to be a protonated Schiff base. Electron delocalization appears to play the dominant role in color regulation. The dark-adapted spectrum indicates a conformation closer to 13-cis than the light-adapted spectrum.

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Year:  1979        PMID: 427199     DOI: 10.1016/0005-2795(79)90417-3

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  5 in total

Review 1.  Microbial and animal rhodopsins: structures, functions, and molecular mechanisms.

Authors:  Oliver P Ernst; David T Lodowski; Marcus Elstner; Peter Hegemann; Leonid S Brown; Hideki Kandori
Journal:  Chem Rev       Date:  2013-12-23       Impact factor: 60.622

2.  Resonance Raman spectra of the acidified and deionized forms of bacteriorhodopsin.

Authors:  S O Smith; R A Mathies
Journal:  Biophys J       Date:  1985-02       Impact factor: 4.033

3.  High-pressure near-infrared Raman spectroscopy of bacteriorhodopsin light to dark adaptation.

Authors:  A Schulte; L Bradley
Journal:  Biophys J       Date:  1995-10       Impact factor: 4.033

4.  Fourier transform infrared difference spectroscopy of bacteriorhodopsin and its photoproducts.

Authors:  K Bagley; G Dollinger; L Eisenstein; A K Singh; L Zimányi
Journal:  Proc Natl Acad Sci U S A       Date:  1982-08       Impact factor: 11.205

5.  Effect of high pressure on the absorption spectrum and isomeric composition of bacteriorhodopsin.

Authors:  M Tsuda; T G Ebrey
Journal:  Biophys J       Date:  1980-04       Impact factor: 4.033

  5 in total

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