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Cited by 22

The DOI matches its Crossref record; 53 of the 53 references it cites were found in a registry or an index.

Assignment of groups responsible for the "opsin shift" and light absorptions of rhodopsin and red, green, and blue iodopsins (cone pigments).

Kosower, E M·1988·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.85.4.1076
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Abstract

A modified structural model of rhodopsin is presented. Seven (alpha-helical) segments of 24 largely hydrophobic amino acid residues are assembled with exobilayer connecting strands into an aligned set, using the sequences of human red, green, and blue iodopsins (cone pigments) and human and bovine rod rhodopsins. (Aligned set numbering is used in this article). The inner region of the heptahelical hydrophobic domain includes one His-Glu (Asp) ion pair (red, green rod) near the retinylidene moiety in addition to an iminium ion Asp-99 pair. The negative charges posited in the "point-charge model" to cause the shift of the retinylidene iminium ion light absorption to longer wavelengths in the protein ("opsin shift") are Asp-99 (red, green rod), Glu-102 (red, green), and Glu-138 (rod). Blue iodopsin lacks both an ion pair and a counter charge to the iminium ion in the inner region, a fact that explains its absorption relative to rod rhodopsin. The spectroscopic difference between rod rhodopsin and the red/green iodopsins is due to the influence of Glu-102 in the latter. The red-green difference is due to the net effect of seven OH groups around the chromophore, all such groups being found within one helix turn of the retinylidene location. The tryptophan, which rotates as the retinylidene group isomerizes, may be Trp-142 or Trp-177. The geometric change (the rhodopsin "photoswitch") resulting from cis-trans isomerization in the first excited electronic state (S1), ultimately leads to RX (photoactivated rhodopsin, metarhodopsin II) and changes the activity of exobilayer groups, possibly causing dissociation of Lys-83 and Arg-85 from the carboxylate groups at positions 263 and 265.

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Metadata

Authors
Kosower, E. M.
Affiliations
Biophysical Organic Chemistry Unit, School of Chemistry, Sackler Faculty of Exact Sciences, Tel-Aviv University, Ramat-Aviv, Israel.
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
1988-02
Volume
85
Issue
4
Pages
1076-1080
ISSN
  • 0027-8424
  • 1091-6490
DOI
10.1073/pnas.85.4.1076
Cited by
22
References
53
Language
en

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