Comparative study on the chromophore binding sites of rod and red-sensitive cone visual pigments by use of synthetic retinal isomers and analogues

Yoshitaka Fukada, Toshiyuki Okano, Yoshinori Shichida, Tôru Yoshizawa, Achla Trehan, Dennis Mead, Marlene Denny, Alfred E. Asato, Robert S H Liu

Research output: Contribution to journalArticle

58 Citations (Scopus)

Abstract

A comparative study on the chromophore (retinal) binding sites of the opsin (R-photopsin) from chicken red-sensitive cone visual pigment (iodopsin) and that (scotopsin) from bovine rod pigment (rhodopsin) was made by the aid of geometric isomers of retinal (all-trans, 13-cis, 11-cis, 9-cis, and 7-cis) and retinal analogues including fluorinated (14-F, 12-F, 10-F, and 8-F) and methylated (12-methyl) 11-cis-retinals. The stereoselectivity of R-photopsin for the retinal isomers and analogues was almost identical with that of scotopsin, indicating that the shapes of the chromophore binding sites of both opsins are similar, although the former appears to be somewhat more restricted than the latter. The rates of pigment formation from R-photopsin were considerably greater than those from scotopsin. In addition, all the iodopsin isomers and analogues were more susceptible to hydroxylamine than were the rhodopsin ones. These observations suggest that the retinal binding site of iodopsin is located near the protein surface. On the basis of the spectral properties of fluorinated analogues, a polar group in the chromophore binding site of iodopsin as well as rhodopsin was estimated to be located near the hydrogen atom at the C10 position of the retinylidene chromophore. A large difference in wavelength between the absorption maxima of iodopsin and rhodopsin was significantly reduced in the 9-cis and 7-cis pigments. On the assumption that the retinylidene chromophore is anchored rigidly at the α-carbon of the lysine residue and loosely at the cyclohexenyl ring, each of the two isomers would have the Schiff-base nitrogen at a position altered from that of the 11-cis pigments. Thus, the remarkable red-shift in the absorption spectrum of iodopsin as compared with that of rhodopsin could be attributed to a difference between the two pigments in the location of a negative charge directly hydrogen bonded to the Schiff-base nitrogen.

Original languageEnglish
Pages (from-to)3133-3140
Number of pages8
JournalBiochemistry
Volume29
Issue number12
Publication statusPublished - 1990
Externally publishedYes

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Retinal Pigments
Chromophores
Rhodopsin
Isomers
Cones
Pigments
Binding Sites
Opsins
Schiff Bases
Hydrogen
Nitrogen
Stereoselectivity
Hydroxylamine
Lysine
iodopsin
Absorption spectra
Chickens
Membrane Proteins
Carbon
Wavelength

ASJC Scopus subject areas

  • Biochemistry

Cite this

Comparative study on the chromophore binding sites of rod and red-sensitive cone visual pigments by use of synthetic retinal isomers and analogues. / Fukada, Yoshitaka; Okano, Toshiyuki; Shichida, Yoshinori; Yoshizawa, Tôru; Trehan, Achla; Mead, Dennis; Denny, Marlene; Asato, Alfred E.; Liu, Robert S H.

In: Biochemistry, Vol. 29, No. 12, 1990, p. 3133-3140.

Research output: Contribution to journalArticle

Fukada, Y, Okano, T, Shichida, Y, Yoshizawa, T, Trehan, A, Mead, D, Denny, M, Asato, AE & Liu, RSH 1990, 'Comparative study on the chromophore binding sites of rod and red-sensitive cone visual pigments by use of synthetic retinal isomers and analogues', Biochemistry, vol. 29, no. 12, pp. 3133-3140.
Fukada, Yoshitaka ; Okano, Toshiyuki ; Shichida, Yoshinori ; Yoshizawa, Tôru ; Trehan, Achla ; Mead, Dennis ; Denny, Marlene ; Asato, Alfred E. ; Liu, Robert S H. / Comparative study on the chromophore binding sites of rod and red-sensitive cone visual pigments by use of synthetic retinal isomers and analogues. In: Biochemistry. 1990 ; Vol. 29, No. 12. pp. 3133-3140.
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abstract = "A comparative study on the chromophore (retinal) binding sites of the opsin (R-photopsin) from chicken red-sensitive cone visual pigment (iodopsin) and that (scotopsin) from bovine rod pigment (rhodopsin) was made by the aid of geometric isomers of retinal (all-trans, 13-cis, 11-cis, 9-cis, and 7-cis) and retinal analogues including fluorinated (14-F, 12-F, 10-F, and 8-F) and methylated (12-methyl) 11-cis-retinals. The stereoselectivity of R-photopsin for the retinal isomers and analogues was almost identical with that of scotopsin, indicating that the shapes of the chromophore binding sites of both opsins are similar, although the former appears to be somewhat more restricted than the latter. The rates of pigment formation from R-photopsin were considerably greater than those from scotopsin. In addition, all the iodopsin isomers and analogues were more susceptible to hydroxylamine than were the rhodopsin ones. These observations suggest that the retinal binding site of iodopsin is located near the protein surface. On the basis of the spectral properties of fluorinated analogues, a polar group in the chromophore binding site of iodopsin as well as rhodopsin was estimated to be located near the hydrogen atom at the C10 position of the retinylidene chromophore. A large difference in wavelength between the absorption maxima of iodopsin and rhodopsin was significantly reduced in the 9-cis and 7-cis pigments. On the assumption that the retinylidene chromophore is anchored rigidly at the α-carbon of the lysine residue and loosely at the cyclohexenyl ring, each of the two isomers would have the Schiff-base nitrogen at a position altered from that of the 11-cis pigments. Thus, the remarkable red-shift in the absorption spectrum of iodopsin as compared with that of rhodopsin could be attributed to a difference between the two pigments in the location of a negative charge directly hydrogen bonded to the Schiff-base nitrogen.",
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AU - Yoshizawa, Tôru

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AU - Denny, Marlene

AU - Asato, Alfred E.

AU - Liu, Robert S H

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