Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10869973 | FEBS Letters | 2015 | 5 Pages |
Abstract
Histidine kinase rhodopsin 1 is a photoreceptor in green algae functioning as a UV-light sensor. It switches between a UV-absorbing state (Rh-UV) and a blue-absorbing state (Rh-Bl) with a protonated retinal Schiff base (RSB) cofactor in a mixture of 13-trans,15-anti and 13-cis,15-syn isomers. The present spectroscopic study now shows that cofactor-protein assembly stabilizes the protonated 13-trans,15-anti RSB isomer. Formation of the active photoswitch requires the photoinduced conversion to Rh-UV. The transitions between the Rh-Bl isomers and the deprotonated 13-cis,15-anti and 13-trans,15-syn isomers of Rh-UV proceed via multiple photoisomerizations of one or simultaneously two double bonds.
Keywords
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Meike Luck, Sara Bruun, Anke Keidel, Peter Hegemann, Peter Hildebrandt,