Kottke, Tilman and Hegemann, Peter and Dick, Bernhard and Heberle, Joachim (2006) The photochemistry of the light-, oxygen-, and voltage-sensitive domains in the algal blue light receptor phot. Biopolymers 82 (4), pp. 373-378.
Full text not available from this repository.
A review. Phot proteins are blue light photoreceptors in plants and algae that mainly regulate photomovement responses. They contain two light-, oxygen-, and voltage-sensitive (LOV) domains and a serine-threonine kinase domain. Both LOV domains noncovalently bind FMN as chromophore. Upon blue light illumination, the LOV domains undergo a photocycle, transiently forming a covalent adduct of the FMN moiety with a nearby cysteine residue. The presence of two light-sensitive domains in the photoreceptor raises the question about the differences in properties and function between LOV1 and LOV2. As a model system, the photocycles of the LOV1 and LOV2 domains from phot of the green alga Chlamydomonas reinhardtii have been studied in detail, both sep. and in a tandem construct. Here we give an overview about the results on the individual of the domains and their interaction. Furthermore, the current status in the understanding of the role of LOV1 in phot in general is presented.
|Additional information (public):||CAN 145:243273 6-0 General Biochemistry|
|Institutions:||Chemistry and Pharmacy > Institut für Physikalische und Theoretische Chemie > Chair of Chemistry III - Physical Chemistry (Light and Matter) > Prof. Dr. Bernhard Dick|
|Projects:||GRK 640 Sensory photoreceptors in natural and artificial systems, Blaulicht-sensitive Photorezeptoren|
|Keywords:||Protein motifs (LOV (light-, oxygen-, and voltage-sensitive) domain, photochem. anal. addresses role of LOV1 photocycle in tandem arrangement of LOV domains in C. reinhardtii phot protein); Chlamydomonas reinhardtii; Photochemistry (photochem. anal. addresses role of LOV1 photocycle in tandem arrangement of LOV domains in C. reinhardtii phot protein); Phototropins; Role: BSU (Biological study, unclassified), BIOL (Biological study) (photochem. anal. addresses role of LOV1 photocycle in tandem arrangement of LOV domains in C. reinhardtii phot protein); review phot protein Chlamydomonas LOV domain photocycle|
|Subjects:||500 Science > 570 Life sciences|
500 Science > 540 Chemistry & allied sciences
|Refereed:||Yes, this version has been refereed|
|Created at the University of Regensburg:||Partially|
|Owner:||Prof. Dr. Bernhard Dick|
|Deposited On:||15 Jan 2009 17:34|
|Last Modified:||31 Aug 2012 11:14|
- ASCII Citation
- Dublin Core
- HTML Citation
- OAI-ORE Resource Map (Atom Format)
- OAI-ORE Resource Map (RDF Format)
- Reference Manager
- Simple Metadata
Literature of the same author