Activation of Chlamydomonas Rhodopsin in Vivo Does Not Require Isomerization of Retinal

Kenneth W. Foster; Jureepan Saranak; Fadila Derguini; Gerald R. Zarrilli; Randy Johnson; Masami Okabe; Koji Nakanishi

doi:10.1021/bi00428a061

Activation of Chlamydomonas Rhodopsin in Vivo Does Not Require Isomerization of Retinal

Kenneth W. Foster, Jureepan Saranak, Fadila Derguini, Gerald R. Zarrilli, Randy Johnson, Masami Okabe, Koji Nakanishi

Department of Physics

Research output: Contribution to journal › Article › peer-review

42 Scopus citations

Abstract

The unicellular eukaryote Chlamydomonas reinhardtii is a phototactic alga that swims toward or away from light, using rhodopsin as the photopigment. The activity of retinal analogues was tested in the mutant FN68, which has high phototactic sensitivity only after incubation with retinal or analogues of retinal. Analogues prevented from isomerizing about the 7-ene, 9-ene, 11-ene, 13-ene, or 15-ene (C=N⁺H) bonds retained full activity. Also, bleaching, protonation of the N, and a stable geometrically altered chromophore are not required for full activity. An attractive hypothesis is that charge redistribution in the excited state of retinal directly triggers the activity of rhodopsin.

Original language	English (US)
Pages (from-to)	819-824
Number of pages	6
Journal	Biochemistry
Volume	28
Issue number	2
DOIs	https://doi.org/10.1021/bi00428a061
State	Published - 1989

ASJC Scopus subject areas

Biochemistry

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title = "Activation of Chlamydomonas Rhodopsin in Vivo Does Not Require Isomerization of Retinal",

abstract = "The unicellular eukaryote Chlamydomonas reinhardtii is a phototactic alga that swims toward or away from light, using rhodopsin as the photopigment. The activity of retinal analogues was tested in the mutant FN68, which has high phototactic sensitivity only after incubation with retinal or analogues of retinal. Analogues prevented from isomerizing about the 7-ene, 9-ene, 11-ene, 13-ene, or 15-ene (C=N+H) bonds retained full activity. Also, bleaching, protonation of the N, and a stable geometrically altered chromophore are not required for full activity. An attractive hypothesis is that charge redistribution in the excited state of retinal directly triggers the activity of rhodopsin.",

author = "Foster, {Kenneth W.} and Jureepan Saranak and Fadila Derguini and Zarrilli, {Gerald R.} and Randy Johnson and Masami Okabe and Koji Nakanishi",

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volume = "28",

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T1 - Activation of Chlamydomonas Rhodopsin in Vivo Does Not Require Isomerization of Retinal

AU - Foster, Kenneth W.

AU - Saranak, Jureepan

AU - Derguini, Fadila

AU - Zarrilli, Gerald R.

AU - Johnson, Randy

AU - Okabe, Masami

AU - Nakanishi, Koji

PY - 1989

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N2 - The unicellular eukaryote Chlamydomonas reinhardtii is a phototactic alga that swims toward or away from light, using rhodopsin as the photopigment. The activity of retinal analogues was tested in the mutant FN68, which has high phototactic sensitivity only after incubation with retinal or analogues of retinal. Analogues prevented from isomerizing about the 7-ene, 9-ene, 11-ene, 13-ene, or 15-ene (C=N+H) bonds retained full activity. Also, bleaching, protonation of the N, and a stable geometrically altered chromophore are not required for full activity. An attractive hypothesis is that charge redistribution in the excited state of retinal directly triggers the activity of rhodopsin.

AB - The unicellular eukaryote Chlamydomonas reinhardtii is a phototactic alga that swims toward or away from light, using rhodopsin as the photopigment. The activity of retinal analogues was tested in the mutant FN68, which has high phototactic sensitivity only after incubation with retinal or analogues of retinal. Analogues prevented from isomerizing about the 7-ene, 9-ene, 11-ene, 13-ene, or 15-ene (C=N+H) bonds retained full activity. Also, bleaching, protonation of the N, and a stable geometrically altered chromophore are not required for full activity. An attractive hypothesis is that charge redistribution in the excited state of retinal directly triggers the activity of rhodopsin.

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Activation of Chlamydomonas Rhodopsin in Vivo Does Not Require Isomerization of Retinal

Abstract

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