Literature DB >> 11938670

Energy transfer from tryptophane amino acid residues to retinal in a bacteriorhodopsin molecule within a femtosecond timescale.

O A Dzhemesyuk1, S A Antipin, F E Gostev, I B Fedorovich, O M Sarkisov, M A Ostrovskii.   

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Year:  2002        PMID： 11938670     DOI： 10.1023/a:1014411424849

Source DB:  PubMed          Journal:  Dokl Biochem Biophys        ISSN： 1607-6729            Impact factor:   0.788


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  9 in total

Review 1.  Closing in on bacteriorhodopsin: progress in understanding the molecule.

Authors:  U Haupts; J Tittor; D Oesterhelt
Journal:  Annu Rev Biophys Biomol Struct       Date:  1999

Review 2.  Nature of the primary photochemical events in rhodopsin and bacteriorhodopsin.

Authors:  R R Birge
Journal:  Biochim Biophys Acta       Date:  1990-04-26

3.  Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane.

Authors:  D Oesterhelt; W Stoeckenius
Journal:  Methods Enzymol       Date:  1974       Impact factor: 1.600

4.  Intramolecular energy transfer in rhodopsin.

Authors:  A Kropf
Journal:  Vision Res       Date:  1967-11       Impact factor: 1.886

5.  Ultraviolet and visible absorption spectra of the purple membrane protein and the photocycle intermediates.

Authors:  B Becher; F Tokunaga; T G Ebrey
Journal:  Biochemistry       Date:  1978-06-13       Impact factor: 3.162

6.  Alkaline quenching of bacteriorhodopsin tryptophanyl fluorescence: evidence for aqueous accessibility or a hydrogen-bonded chain.

Authors:  P L Palmer; W V Sherman
Journal:  Photochem Photobiol       Date:  1985-11       Impact factor: 3.421

7.  Rhodopsin-like protein from the purple membrane of Halobacterium halobium.

Authors:  D Oesterhelt; W Stoeckenius
Journal:  Nat New Biol       Date:  1971-09-29

8.  Photochemistry and fluorescence of bacteriorhodopsin excited in its 280-nm absorption band.

Authors:  O Kalisky; J Feitelson; M Ottolenghi
Journal:  Biochemistry       Date:  1981-01-06       Impact factor: 3.162

9.  Tryptophan fluorescence quenching as a monitor for the protein conformation changes occurring during the photocycle of bacteriorhodopsin under different perturbations.

Authors:  D J Jang; M A el-Sayed
Journal:  Proc Natl Acad Sci U S A       Date:  1989-08       Impact factor: 11.205
  9 in total

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