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Biophysical Journal 35: 543-546 (1981)
© 1981 the Biophysical Society

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Flash photolysis and low temperature photochemistry of bovine rhodopsin with a fixed 11-ene.

B Mao, M Tsuda, T G Ebrey, H Akita, V Balogh-Nair and K Nakanishi

ABSTRACT

Nonbleachable rhodopsins containing retinal moieties with fixed 11-ene structures have been prepared. When the nonbleachable rhodopsin analogue corresponding to the natural pigment was flash-photolysed at 20.8 degrees C, no absorption changes occurred at the monitoring wavelengths of 380, 480, and 580 nm for the time range of 2 microseconds--10 s. This observation is in contrast to that of natural rhodopsin which showed the formation of metarhodopsin I and its decay to meta II. Irradiation of the artificial rhodopsin, 77 K, with light of 460 and 540 nm, also gave no spectral changes; in the case of natural rhodopsin, however, the irradiation leads to formation of the red-shifted intermediate bathorhodopsin. The absence of photochemistry in the artificial pigment shows that an 11-cis to trans photoisomerization of the retinal moiety is a crucial step in inducing the chain of events in te photolysis of rhodopsin.




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Proc. Natl. Acad. Sci. USAHome page
M. Nakagawa, T. Iwasa, S. Kikkawa, M. Tsuda, and T. G. Ebrey
How vertebrate and invertebrate visual pigments differ in their mechanism of photoactivation
PNAS, May 25, 1999; 96(11): 6189 - 6192.
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Copyright © 1981 by the Biophysical Society.