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

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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 languageEnglish (US)
Pages (from-to)819-824
Number of pages6
JournalBiochemistry
Volume28
Issue number2
DOIs
StatePublished - Jan 1 1989

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ASJC Scopus subject areas

  • Biochemistry

Cite this

Foster, K. W., Saranak, J., Derguini, F., Zarrilli, G. R., Johnson, R., Okabe, M., & Nakanishi, K. (1989). Activation of Chlamydomonas Rhodopsin in Vivo Does Not Require Isomerization of Retinal. Biochemistry, 28(2), 819-824. https://doi.org/10.1021/bi00428a061