TY  - JOUR
AU  - Kottke, T.
AU  - Heberle, J.
AU  - Hehn, D.
AU  - Dick, B.
AU  - Hegemann, P.
TI  - Phot-LOV1 : photocycle of a blue-light receptor domain from the green alga Chlamydomonas reinhardtii
JO  - Biophysical journal
VL  - 84
SN  - 0006-3495
CY  - New York, NY
PB  - Rockefeller Univ. Press
M1  - PreJuSER-26841
SP  - 1192 - 1201
PY  - 2003
N1  - Record converted from VDB: 12.11.2012
AB  - The "Phot" protein family comprises blue-light photoreceptors that consist of two flavin mononucleotide (FMN)binding LOV (light, oxygen, and voltage) domains and a serine/threonine kinase domain. We have investigated the LOV1 domain of Phot1 from Chlamydomonas reinhardtii by time-resolved absorption spectroscopy. Photoexcitation of the dark form, LOV1-447, causes transient bleaching and formation of two spectrally similar red-shifted intermediates that are both assigned to triplet states of the FMN. The triplet states decay with time constants of 800 ns and 4 mus with an efficiency of >90% into a blue-shifted intermediate, LOV1-390, that is attributed to a thiol adduct of cysteine 57 to FMN C(4a). LOV1-390 reverts to the dark form in hundreds of seconds, the time constant being dependent on pH and salt concentration. In the mutant C57S, where the thiol adduct cannot be formed, the triplet state displays an oxygen-dependent decay directly to the dark form. We present here a spectroscopic characterization of an algal sensory photoreceptor in general and of a LOV1 domain photocycle in particular. The results are discussed with respect to the behavior of the homologous LOV2 domain from oat.
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000183123700042
UR  - https://juser.fz-juelich.de/record/26841
ER  -