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The photochemistry of the light‐, oxygen‐, and voltage‐sensitive domains in the algal blue light receptor phot
Author(s) -
Kottke Tilman,
Hegemann Peter,
Dick Bernhard,
Heberle Joachim
Publication year - 2006
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20510
Subject(s) - chemistry , photochemistry , blue light , oxygen , biophysics , optoelectronics , physics , organic chemistry , biology
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 a flavin mononucleotide (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 separately and in a tandem construct. Here we give an overview about the results on the individual behavior of the domains and their interaction. Furthermore, the current status in the understanding of the role of LOV1 in phot in general is presented. © 2006 Wiley Periodicals, Inc. Biopolymers 82: 373–378, 2006 This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com