34 CHEMICAL MODIFICATION OF RETINAL MOIETY IN PURPLE MEMBRANE

DOI
  • Tsujimoto K.
    Department of Materials Science, The University of Electro-Communications
  • Tokunaga F.
    Department of Physics, Tohoku University
  • Balogh-Nair V.
    Department of Chemistry, Columbia University
  • Nakanishi K.
    Department of Chemistry, Columbia University
  • Watanabe M.
    National Institute for Basic Biology, Okazaki National Research Institute
  • Hattori H.
    National Institute for Basic Biology, Okazaki National Research Institute

Bibliographic Information

Other Title
  • 34 高度好塩菌の紫膜におけるレチナールアナログを用いる光受容

Description

The purpose of this study on photoreception of modified bacteriorhodopsins involves obtaining information on the structure of the protein by chemically analyzing bacteriorhodopsins which are reconstituted with artificial retinals and the opsin, and by comparison of their properties with these of the native bacteriorhodopsin. We report structural contribution of the protein to the bathochromic shifts and photochemical behavior of artificial bacteriorhodopsin. 1) Hydroretinals and hydrorhodopsins were synthesized to investigate the protein circumstances. 'Opsin shift', one of the indicator, was defined as λ_<max> of the protonated Schiff base of n-butylamine minus λ_<max> of the corresponding pigment (cm^<-1>). Point charge model was proposed that another anion except a counter ion of the Schiff base would be located not on the side chain but near the cyclohexene ring. 2) Modification of cyclohexene ring to phenyl ring strongly affected the opsin shift, while introduction of bromine atom to side chain was less effective. 3) Irradiation upon bacteriorhodopsin involving Np-retinal gave rise to anomalous photoisomerization of retinal moiety.

Journal

Details 詳細情報について

  • CRID
    1390001206073294976
  • NII Article ID
    110006678238
  • DOI
    10.24496/tennenyuki.24.0_261
  • ISSN
    24331856
  • Text Lang
    ja
  • Data Source
    • JaLC
    • CiNii Articles
  • Abstract License Flag
    Disallowed

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