Abstract
In vertebrate visual pigments, a glutamic acid serves as a negative counterion to the positively charged chromophore, a protonated Schiff base of retinal. When photoisomerization leads to the Schiff base deprotonating, the anionic glutamic acid becomes protonated, forming a neutral species that activates the visual cascade. We show that in octopus rhodopsin, the glutamic acid has no anionic counterpart. Thus, the "counterion" is already neutral, so no protonated form of an initially anionic group needs to be created to activate. This helps to explain another observation-that the active photoproduct of octopus rhodopsin can be formed without its Schiff base deprotonating. In this sense, the mechanism of light activation of octopus rhodopsin is simpler than for vertebrates, because it eliminates one of the steps required for vertebrate rhodopsins to achieve their activating state.
MeSH Terms
Amino Acid Sequence
Animals
Humans
Isomerism
Light
Microvilli/physiology
Molecular Sequence Data
Octopodiformes
Photoreceptor Cells, Invertebrate/physiology
Retinal Pigments/chemistry,physiology
Rhodopsin/chemistry,physiology,radiation effects
Schiff Bases
Sequence Alignment
Sequence Homology, Amino Acid
Species Specificity
Spectrophotometry
Vertebrates
Vision, Ocular/physiology
Chemicals
Retinal Pigments
Schiff Bases
Rhodopsin
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Nakagawa M
Department of Life Science, Himeji Institute of Technology, Harima Science Garden City, Akoh-gun, Hyogo 678-1297, Japan.
Iwasa T
Kikkawa S
Tsuda M
Ebrey T G
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