Carotenoids pp 75-104 | Cite as


  • J. B. C. Findlay
  • D. J. C. Pappin
  • M. Brett
  • P. F. Zagalsky


At the 6th International Symposium on Carotenoids in Liverpool (1981), Britton1 gave a survey of the information obtainable in using spectroscopic techniques (resonance Raman, circular dichroism etc.) on animal carotenoproteins, in particular on the carotenoid-protein interaction. The separate specificities of carotenoid attachment for several carotenoproteins, evident in the extensive work emanating from his laboratory on the reconstitution of several pigments, with a varied range of both natural and synthetic carotenoids, were detailed. A wealth of data was extracted from the studies both on the prerequisites of carotenoid structure for binding and the relevance of specific parts of the molecule in the accompanying spectral change as, for example, the importance of a conjugated 4-keto group and C-13,13’ methyl groups for purple/blue carotenoproteins. Speculation on the mechanism for the large bathochromic shift in the absorption spectrum of the carotenoid in the latter type of pigment, crustacyanin, the lobster carapace astaxanthin(I)-protein, being a typical example, has been amply dwelt on previously2: some form of polarisation mechanism3, for which there is substantial support and general acceptance for the spectrally analogous rhodopsin class of pigments4–6 would seem reasonable on present evidence in the absence of any definitive verification.


Circular Dichroism Circular Dichroism Spectrum Common Ancestry Residue Number Central Residue 
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Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • J. B. C. Findlay
    • 1
  • D. J. C. Pappin
    • 1
  • M. Brett
    • 1
  • P. F. Zagalsky
    • 2
  1. 1.Department of BiochemistryUniversity of LeedsLeedsUK
  2. 2.Department of BiochemistryRoyal Holloway and Bedford New CollegeEgham, SurreyUK

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