Photoisomerization in Rhodopsin
Abstract
This article reviews the primary reaction processes in rhodopsin, a photoreceptive pigment for twilight vision. Rhodopsin has an 11-cis retinal as the chromophore, which binds covalently with a lysine residue through a protonated Schiff base linkage. Absorption of a photon by rhodopsin initiates the primary photochemical reaction in the chromophore. Picosecond time-resolved spectroscopy of 11-cis locked rhodopsin analogs revealed that the cis-trans isomerization of the chromophore is the primary reaction in rhodopsin. Then, generation of femtosecond laser pulses in the 1990s made it possible to follow the process of isomerization in real time. Formation of photorhodopsin within 200 fsec was observed by a transient absorption (pump-probe) experiment, which also revealed that the photoisomerization in rhodopsin is a vibrationally coherent process. Femtosecond fluorescence spectroscopy directly captured excited-state dynamics of rhodopsin, so that both coherent reaction process and unreacted excited state were observed. Faster photoreaction of the chromophore in rhodopsin than that in solution implies that the protein environment facilitates the efficient isomerization process. Such contributions of the protein residues have been monitored by infrared spectroscopy of rhodopsin, bathorhodopsin, and isorhodopsin (9-cis rhodopsin) at low temperatures. The crystal structure of bovine rhodopsin recently reported will lead to better understanding of the mechanism in future.
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Illumination of rhodopsin at its 500 nm maximum causes the chromophore to undergo geometrical isomerization.
“Upon illumination of rhodopsin (λmax = 500 nm), the chromophore undergoes geometrical isomerization.”
From Chemistry of the Retinoid (Visual) Cycle (2014) · cites this paper as [356]
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- Authors
- Kandori, H., Shichida, Y., & Yoshizawa, T.
- Affiliations
- Kyoto University (JP)
- Nagoya Institute of Technology (JP)
- Corresponding author
- Kandori, H.
- Venue
- Biochemistry (Moscow)
- Published
- 2001-11
- Volume
- 66
- Issue
- 11
- Pages
- 1197-1209
- ISSN
- 0006-2979 (ISSN-L)
- 1608-3040
- OpenAlex
- W2143636398
- Cited by
- 220
- References
- 71
- Citations by year
- 2026: 5 · 2025: 4 · 2024: 8 · 2023: 7 · 2022: 3 · 2021: 8 · 2020: 10 · 2019: 10 · 2018: 7 · 2017: 9 · 2016: 8 · 2015: 9 · 2014: 12 · 2013: 6 · 2012: 12
- FWCI
- 0.48
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Biochemistry (Moscow) (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Photoreceptor and optogenetics research
- Physical Sciences › Chemistry › Physical and Theoretical Chemistry › Photochemistry and Electron Transfer Studies
- Physical Sciences › Materials Science › Materials Chemistry › Photochromic and Fluorescence Chemistry
- Keywords
- rhodopsin, photoisomerization, 11-cis-retinal, cis-trans isomerization, Schiff base, bathorhodopsin, isorhodopsin, excited-state dynamics, protein environment, twilight vision
- MeSH terms
- Amino Acid Sequence, Animals, Cattle, Isomerism, Molecular Sequence Data, Photochemistry, Rhodopsin, Protein Structure, Secondary, Crystallography, X-Ray
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