Abstract

Ultrafast reverse photoreaction of visual pigment rhodopsin in the femtosecond time range at room temperature is demonstrated. Femtosecond two-pump probe experiments with a time resolution of 25 fs have been performed. The first pump pulse at 500 nm initiated cis-trans photoisomerization of rhodopsin chromophore, 11-cis retinal, which resulted in the formation of the primary ground-state photoproduct within a mere 200 fs. The second pump pulse at 620 nm with a varying delay of 200 to 3750 fs relative to the first pump pulse, initiated the reverse phototransition of the primary photoproduct to rhodopsin. The results of this photoconversion have been observed on the differential spectra obtained after the action of two pump pulses at a time delay of 100 ps. It was found that optical density decreased at 560 nm in the spectral region of bathorhodopsin absorption and increased at 480 nm, where rhodopsin absorbs. Rhodopsin photoswitching efficiency shows oscillations as a function of the time delay between two pump pulses. The quantum yield of reverse photoreaction initiated by the second pump pulse falls within the range 15% ± 1%. The molecular mechanism of the ultrafast reversible photoreaction of visual pigment rhodopsin may be used as a concept for the development of an ultrafast optical molecular switch.

Highlights

  • Retinal-binding proteins form a group of photosensitive transmembrane proteins capable of converting the energy of light to perform biological functions of the living organisms

  • It is shown that photochromic switching efficiency depends on the timing of oscillation maximum for the dynamics of the coherent vibrational wave packet of Photo570 and pump2

  • Such dependence is the obvious example of coherent control over the reverse photoreaction of

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Summary

Introduction

Retinal-binding proteins form a group of photosensitive transmembrane proteins capable of converting the energy of light to perform biological functions of the living organisms This group comprises sensor rhodopsins that provide light perception as an information carrier (visual pigments of animals, sensor rhodopsins of microorganisms) and those performing photovoltaic energetic function, targeting ion transport through the cellular membrane (e.g., halorhodopsin, bacteriorhodopsin) [1,2]. These pigment-protein complexes have a similar spatial organization and common chromophore group: the retinal (vitamin A aldehyde) residue, which is covalently bound to protein through a protonated Schiff base linkage to a lysine residue from the polypeptide chain of protein [3,4]. Ever-increasing interest in the detailed study of photochemical transformation mechanisms of retinal-binding proteins is observed for the purpose of using the functional principles of these natural photosensors in the creation of fast response devices [12,13,14,15,16,17]

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