Light Damaging Action of all-trans-Retinal and Its Derivatives on Rhodopsin Molecules in the Photoreceptor Membrane

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M. Yu. Loginova^*, Ye. V. Rostovtseva, T. B. Feldman, and M. A. Ostrovsky

Emanuel' Institute of Biochemical Physics, Russian Academy of Sciences, ul. Kosygina 4, 119334 Moscow, Russia; fax: (495) 137-4101; E-mail: marina.loguinova@mail.ru

^* To whom correspondence should be addressed.

Received July 13, 2007; Revision received October 8, 2007

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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.

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KEY WORDS: visual pigment rhodopsin, all-trans-retinal, photosensitizers, photodamage

DOI: 10.1134/S000629790802003X

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