2004
DOI: 10.1016/j.chemphys.2004.03.017
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Absorption and emission spectroscopic characterisation of the LOV2-domain of phot from Chlamydomonas reinhardtii fused to a maltose binding protein

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Cited by 30 publications
(37 citation statements)
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“…This modification may come from the structural interaction of LOV1 with LOV2 in which LOV1 may prolong the t1 ⁄ 2 of S390 in LOV2 by acting as a weight on the photoreaction, therefore, preventing the conformational change of LOV2. A similar weight effect was observed with the truncated LOV2 of Cr phot fused with calmodulin-binding protein (44).…”
Section: Discussionsupporting
confidence: 57%
“…This modification may come from the structural interaction of LOV1 with LOV2 in which LOV1 may prolong the t1 ⁄ 2 of S390 in LOV2 by acting as a weight on the photoreaction, therefore, preventing the conformational change of LOV2. A similar weight effect was observed with the truncated LOV2 of Cr phot fused with calmodulin-binding protein (44).…”
Section: Discussionsupporting
confidence: 57%
“…The observed charge-transfer dynamics and energy transfer dynamics may be helpful in elucidating the processes occurring in the photo-cycle dynamics of blue-light photoreceptors [31,32,37,39,42,43,[48][49][50]53,55,56,60,106,107]. The presented studies may also be of interest for molecular electronics applications like fast switching and photovoltaics [12,13,15,16].…”
Section: Discussionmentioning
confidence: 93%
“…They are responsible for plant growth towards light (phototropism). Blue-light excitation causes FMN-C4a-cysteinyl adduct formation mediated via triplet state formation and photo-induced singlet-state reductive electron transfer [42][43][44].…”
Section: Introductionmentioning
confidence: 99%
“…In flavin-cofactor-based blue-light photoreceptors [3,4] (phototropins [7], cryptochromes [8], BLUF domains [9]) efficient flavin fluorescence quenching is observed in the dark-adapted (receptor) state and in the light-adapted (signalling) state (for phototropins see [10,11], for cryptochromes see [12], for BLUF proteins see [13][14][15][16]). This fluorescence quenching is thought to be caused by photoinduced reductive electron transfer from an adjacent amino acid residue (tyrosine, tryptophan, phenylalanine, cysteine, and histidine are known as electron donors for photoexcited flavins [17]) to the excited flavin moiety.…”
Section: Introductionmentioning
confidence: 99%