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Photopsin

Photopsins are photoreceptor proteins found in cone cells of the retina that allow for color vision. There are three main types of photopsins in humans - photopsin I, II, and III - which absorb red, green, and blue-violet light respectively. Photopsins consist of a protein component and a chromophore called retinal. When retinal isomerizes due to light absorption, it causes a conformational change in the protein and activates the photopsin, triggering a signaling cascade. George Wald won the 1967 Nobel Prize in Physiology or Medicine for experiments in the 1950s demonstrating the difference in light absorption by these three photopsins.

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458 views3 pages

Photopsin

Photopsins are photoreceptor proteins found in cone cells of the retina that allow for color vision. There are three main types of photopsins in humans - photopsin I, II, and III - which absorb red, green, and blue-violet light respectively. Photopsins consist of a protein component and a chromophore called retinal. When retinal isomerizes due to light absorption, it causes a conformational change in the protein and activates the photopsin, triggering a signaling cascade. George Wald won the 1967 Nobel Prize in Physiology or Medicine for experiments in the 1950s demonstrating the difference in light absorption by these three photopsins.

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Photopsin

From Wikipedia, the free encyclopedia


(Redirected from Iodopsin)

Normalised absorption spectra of the three human photopsins and of human rhodopsin
(dashed).
Photopsins (also known as Cone opsins) are the photoreceptor proteins found in the cone
cells of the retina that are the basis of color vision. Iodopsin, the cone pigment system in
chicken retina, is a close analog of the visual purple rhodopsin that is used in night vision.
Iodopsin consists of the protein component and a bound chromophore, retinal.

Contents

1 Function

2 Types

3 History

4 See also

5 References

6 External links

Function
Opsins are Gn-x protein-coupled receptors of the retinylidene protein family. Isomerization of
11-cis-retinal into all-trans-retinal by light induces a conformational change in the protein that
activates photopsin and promotes its binding to G protein transducin, which triggers a second
messenger cascade.

Types
Different opsins differ in a few amino acids and absorb light at different wavelengths as
retinal-bound pigments.
Cone type
S (OPN1SW) - "tritan", "cyanolabe"
M (OPN1MW) - "deutan", "chlorolabe"
L (OPN1LW) - "protan", "erythrolabe"

Name
Range
Peak wavelength[1][2]

400500 nm 420440 nm

450630 nm 534545 nm

500700 nm 564580 nm

In humans there are 3 different iodopsins (rhodopsin analogs) that contain the proteinpigment complexes photopsin I, II, and III.
The 3 types of iodopsins are called erythrolabe(photopsin I + retinal), chlorolabe(photopsin
II + retinal), and cyanolabe(photopsin III + retinal).[3]
These photopsins have absorption maxima for red ["erythr"-red] (photopsin I), green
["chlor"-green] (photopsin II), and bluish-violet light ["cyan"-bluish violet] (photopsin III).

History
George Wald received the 1967 Nobel Prize in Physiology or Medicine for his experiments in
the 1950s that showed the difference in absorbance by these photopsins (see image).[4]

See also

Rhodopsins, the pigment for monochromatic (scotopic) dark vision.

Melanopsin, the pigment which is used to control pupil sizes and the sleep/wake cycle

Visual cycle, the chemistry of phototransduction

Color blindness

References
1.
Wyszecki, Gnther; Stiles, W.S. (1982). Color Science: Concepts and Methods, Quantitative
Data and Formulae (2nd ed.). New York: Wiley Series in Pure and Applied Optics. ISBN 0471-02106-7.
R. W. G. Hunt (2004). The Reproduction of Colour (6th ed.). Chichester UK: Wiley
IS&T Series in Imaging Science and Technology. pp. 1112. ISBN 0-470-02425-9.
Rushton, W. A. H. (1 June 1966). "Densitometry of pigments in rods and cones of normal
and color defective subjects" (PDF). Investigative Ophthalmology 5 (3): 233241.
PMID 5296487. Retrieved 2006-11-14.

The Nobel Foundation. "The Nobel Prize in Physiology or Medicine 1967". Nobelprize.org.
Nobel Media AB 2014. Retrieved 12 December 2015.

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