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@ARTICLE{Kottke:26841,
author = {Kottke, T. and Heberle, J. and Hehn, D. and Dick, B. and
Hegemann, P.},
title = {{P}hot-{LOV}1 : photocycle of a blue-light receptor domain
from the green alga {C}hlamydomonas reinhardtii},
journal = {Biophysical journal},
volume = {84},
issn = {0006-3495},
address = {New York, NY},
publisher = {Rockefeller Univ. Press},
reportid = {PreJuSER-26841},
pages = {1192 - 1201},
year = {2003},
note = {Record converted from VDB: 12.11.2012},
abstract = {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.},
keywords = {J (WoSType)},
cin = {IBI-2},
ddc = {570},
cid = {I:(DE-Juel1)VDB58},
pnm = {Neurowissenschaften},
pid = {G:(DE-Juel1)FUEK255},
shelfmark = {Biophysics},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000183123700042},
url = {https://juser.fz-juelich.de/record/26841},
}