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Photochemical chromophore isomerization in histidine kinase rhodopsin HKR1. 2015

Meike Luck, and Sara Bruun, and Anke Keidel, and Peter Hegemann, and Peter Hildebrandt
Humboldt Universität zu Berlin, Institut für Biologie, Experimentelle Biophysik, Invalidenstr. 42, D-10115 Berlin, Germany.

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.

UI MeSH Term Description Entries
D010940 Plant Proteins Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which PLANT PROTEINS, DIETARY is available. Plant Protein,Protein, Plant,Proteins, Plant
D011494 Protein Kinases A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein. Protein Kinase,Kinase, Protein,Kinases, Protein
D000071677 Histidine Kinase A member of the transferase superfamily of proteins. In the activated state, protein-histidine kinase autophosphorylates at a histidine residue, subsequently transferring high-energy phosphoryl groups to an aspartate residue of the response-regulator domain, which results in a conformational shift in the effector domain. Histidine kinases mediate signal transduction in a wide range of processes involving cellular adaptation to environmental stress. Histidine Protein Kinase,Histone H4 Histidine Kinase,Protein Histidine Pros-Kinase,Protein Kinase (Histidine), Pros-Kinase,Protein-Histidine Kinase,Protein-Histidine Pros-Kinase,Protein-Histidine Tele-Kinase,Sensor Histidine Kinase,Histidine Kinase, Sensor,Histidine Pros-Kinase, Protein,Kinase, Histidine,Kinase, Histidine Protein,Kinase, Protein-Histidine,Kinase, Sensor Histidine,Pros-Kinase, Protein Histidine,Pros-Kinase, Protein-Histidine,Protein Histidine Kinase,Protein Histidine Pros Kinase,Protein Histidine Tele Kinase,Protein Kinase, Histidine,Tele-Kinase, Protein-Histidine
D012172 Retinaldehyde A diterpene derived from the carotenoid VITAMIN A which functions as the active component of the visual cycle. It is the prosthetic group of RHODOPSIN (i.e., covalently bonded to ROD OPSIN as 11-cis-retinal). When stimulated by visible light, rhodopsin transforms this cis-isomer of retinal to the trans-isomer (11-trans-retinal). This transformation straightens-out the bend of the retinal molecule and causes a change in the shape of rhodopsin triggering the visual process. A series of energy-requiring enzyme-catalyzed reactions convert the 11-trans-retinal back to the cis-isomer. 11-trans-Retinal,3,7-dimethyl-9-(2,6,6-trimethyl-1-cyclohexen-1-yl)-2,4,6,8-Nonatetraenal,Axerophthal,Retinal,Retinene,Retinyl Aldehydde,Vitamin A Aldehyde,all-trans-Retinal,11-cis-Retinal,11 cis Retinal,11 trans Retinal,Aldehydde, Retinyl,Aldehyde, Vitamin A,all trans Retinal
D012243 Rhodopsin A purplish-red, light-sensitive pigment found in RETINAL ROD CELLS of most vertebrates. It is a complex consisting of a molecule of ROD OPSIN and a molecule of 11-cis retinal (RETINALDEHYDE). Rhodopsin exhibits peak absorption wavelength at about 500 nm. Visual Purple
D012545 Schiff Bases Condensation products of aromatic amines and aldehydes forming azomethines substituted on the N atom, containing the general formula R-N:CHR. (From Grant & Hackh's Chemical Dictionary, 5th ed) Schiff Base,Base, Schiff,Bases, Schiff
D014466 Ultraviolet Rays That portion of the electromagnetic spectrum immediately below the visible range and extending into the x-ray frequencies. The longer wavelengths (near-UV or biotic or vital rays) are necessary for the endogenous synthesis of vitamin D and are also called antirachitic rays; the shorter, ionizing wavelengths (far-UV or abiotic or extravital rays) are viricidal, bactericidal, mutagenic, and carcinogenic and are used as disinfectants. Actinic Rays,Black Light, Ultraviolet,UV Light,UV Radiation,Ultra-Violet Rays,Ultraviolet Light,Ultraviolet Radiation,Actinic Ray,Light, UV,Light, Ultraviolet,Radiation, UV,Radiation, Ultraviolet,Ray, Actinic,Ray, Ultra-Violet,Ray, Ultraviolet,Ultra Violet Rays,Ultra-Violet Ray,Ultraviolet Black Light,Ultraviolet Black Lights,Ultraviolet Radiations,Ultraviolet Ray
D016825 Chlamydomonas reinhardtii A species of GREEN ALGAE. Delicate, hairlike appendages arise from the flagellar surface in these organisms. Chlamydomonas reinhardii,Chlamydomonas reinhardius,Chlamydomonas reinhardtius,reinhardius, Chlamydomonas,reinhardtii, Chlamydomonas

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