Accelerated Publication

Biochemistry (Moscow)

, Volume 73, Issue 2, pp 130-138

First online:

Light damaging action of all-trans-retinal and its derivatives on rhodopsin molecules in the photoreceptor membrane

  • M. Yu. LoginovaAffiliated withEmanuel’ Institute of Biochemical Physics, Russian Academy of Sciences Email author 
  • , Ye. V. RostovtsevaAffiliated withEmanuel’ Institute of Biochemical Physics, Russian Academy of Sciences
  • , T. B. FeldmanAffiliated withEmanuel’ Institute of Biochemical Physics, Russian Academy of Sciences
  • , M. A. OstrovskyAffiliated withEmanuel’ Institute of Biochemical Physics, Russian Academy of Sciences

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Abstract

We have reproduced the model system containing A2-rhodopsin, NR-PE, A2-PE, and ATR-dimer-PE in order to study photosensitized damage of rhodopsin within photoreceptor membranes of rod outer segments. We have demonstrated that irradiation of such a system with visible light (400–700 nm) distorts the most important functional property of native visual pigment—its ability to regenerate after addition of 11-cis-retinal in the dark. We have also shown that all-trans-retinal bound to membrane phospholipids and rhodopsin has less photosensitizing activity that free all-trans-retinal.

Key words

visual pigment rhodopsin all-trans-retinal photosensitizers photodamage