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. 1988 Jan;53(1):17–24. doi: 10.1016/S0006-3495(88)83061-3

Primary Processes in Photolysis of Octopus Rhodopsin

Hiroyuki Ohtani, Takayoshi Kobayashi, Motoyuki Tsuda, Thomas G Ebrey
PMCID: PMC1330117  PMID: 19431715

Abstract

The photolysis of octopus rhodopsin was studied by picosecond time-resolved spectroscopy at physiological temperature (8°C) and by steady-state spectroscopy at very low temperature (10 K). Both hypsorhodopsin and bathorhodopsin were formed from a bathorhodopsin-like red-shifted intermediate “primerhodopsin,” which was the primary photoproduct with our time resolution (36 ps). Though it was proposed that hypsorhodopsin is formed solely by a multiphoton process, the present results obtained by using blue light pulses (461 nm) of low intensity showed that hypsorhodopsin is formed by a single photon mechanism via thermal decay from primerhodopsin. When the excitation intensity is increased, a channel for the photochemical formation of hypsorhodopsin from primerhodopsin is opened. There are two thermal pathways leading from primerhodopsin. One process is the formation of hypsorhodopsin, which is later thermally converted to bathorhodopsin, and the other is the direct formation of bathorhodopsin from primerhodopsin. The formation efficiencies at room temperature of hypsorhodopsin and bathorhodopsin at very low excitation intensity were estimated to be larger than 0.6 and smaller than 0.4, respectively. The formation of hypsorhodopsin was also found in the early stages of the irradiation of octopus rhodopsin with weak continuous light at 10 K. However bathorhodopsin is formed three times more efficiently than hypsorhodopsin at 10 K.

At physiological temperatures the formation of hypsorhodopsin in D2O takes place more slowly than in H2O. This indicates that the lifetime of primerhodopsin is decreased by H2O/D2O exchange. The rate constant for the primerhodopsin → bathorhodopsin conversion is more sensitive than that for the primerhodopsin → hypsorhodopsin conversion. The transformation of hypsorhodopsin to bathorhodopsin shows no deuterium effect at low temperature.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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