The two parallel photocycles of the Chlamydomonas sensory photoreceptor histidine kinase rhodopsin 1

Bibliographische Detailangaben
Veröffentlicht in:	Journal of plant physiology. - 1979. - 217(2017) vom: 01. Okt., Seite 77-84
1. Verfasser:	Luck, Meike (VerfasserIn)
Weitere Verfasser:	Hegemann, Peter
Format:	Online-Aufsatz
Sprache:	English
Veröffentlicht:	2017
Zugriff auf das übergeordnete Werk:	Journal of plant physiology
Schlagworte:	Journal Article Review Chlamydomonas reinhardtii Microbial rhodopsin Photocycle Photoreceptor Retinal isomerization Photoreceptors, Plant Rhodopsin 9009-81-8 mehr... Histidine Kinase EC 2.7.13.1

Beschreibung
Zusammenfassung:	Copyright © 2017 Elsevier GmbH. All rights reserved. Histidine kinase rhodopsins (HKRs) belong to a class of unexplored sensory photoreceptors that share a similar modular architecture. The light sensing rhodopsin domain is covalently linked to signal-transducing modules and in some cases to a C-terminal guanylyl-cyclase effector. In spite of their wide distribution in unicellular organisms, very little is known about their physiological role and mechanistic functioning. We investigated the photochemical properties of the recombinant rhodopsin-fragment of Cr-HKR1 originating from Chlamydomonas reinhardtii. Our spectroscopic studies revealed an unusual thermal stability of the photoproducts with the deprotonated retinal Schiff base (RSB). Upon UV-irradiation these Rh-UV states with maximal absorbance in the UVA-region (Rh-UV) photochemically convert to stable blue light absorbing rhodopsin (Rh-Bl) with protonated chromophore. The heterogeneity of the sample is based on two parallel photocycles with the chromophore in C15=N-syn- or -anti-configuration. This report represents an attempt to decipher the underlying reaction schemes and interconversions of the two coexisting photocycles
Beschreibung:	Date Completed 14.03.2018 Date Revised 30.09.2020 published: Print-Electronic Citation Status MEDLINE
ISSN:	1618-1328
DOI:	10.1016/j.jplph.2017.07.008