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000049345 0247_ $$2pmid$$apmid:15879473
000049345 0247_ $$2pmc$$apmc:PMC1366540
000049345 0247_ $$2DOI$$a10.1529/biophysj.104.058230
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000049345 084__ $$2WoS$$aBiophysics
000049345 1001_ $$0P:(DE-HGF)0$$aGuo, H.$$b0
000049345 245__ $$aThe Phot LOLV2 Domain and its Interaction with LOV1
000049345 260__ $$aNew York, NY$$bRockefeller Univ. Press$$c2005
000049345 300__ $$a402 - 412
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000049345 440_0 $$0882$$aBiophysical Journal$$v89$$x0006-3495
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000049345 520__ $$aPhot proteins are homologs of the blue-light receptor phototropin. We report a comparative study of the photocycles of the isolated, light-sensitive domains LOV1 and LOV2 from Chlamydomonas reinhardtii phot protein, as well as the construct LOV1/2 containing both domains. Transient absorption measurements revealed a short lifetime of the LOV2-wt triplet state (500 ns), but a long lifetime (287 micros) of the triplet in the mutant LOV2-C250S, in which the reactive cysteine is replaced by serine. For LOV1, in comparison, corresponding numbers of 800 ns and 4 micros for the two conformers in LOV1-wt, and 27 micros for LOV1-C57S have been reported. The triplet decay kinetics in the mixed domains LOV1/2-wt, LOV1/2-C57S, and LOV1/2-C250S can be analyzed as the superposition of the behavior of the corresponding single domains. The situation is different for the slow, thermal reaction of the photoadduct back to the dark form. Whereas the individual domains LOV1 and LOV2 show two decay components, the double domains LOV1/2-C57S and LOV1/2-C250S both show only a single component. The interaction of the two domains does therefore not manifest itself during the lifetime of the triplet states, but changes the decay behavior of the adduct states.
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000049345 650_2 $$2MeSH$$aAnimals
000049345 650_2 $$2MeSH$$aAnions
000049345 650_2 $$2MeSH$$aCations
000049345 650_2 $$2MeSH$$aChlamydomonas reinhardtii: metabolism
000049345 650_2 $$2MeSH$$aCryptochromes
000049345 650_2 $$2MeSH$$aCysteine: chemistry
000049345 650_2 $$2MeSH$$aDNA Adducts
000049345 650_2 $$2MeSH$$aFlavoproteins: chemistry
000049345 650_2 $$2MeSH$$aHot Temperature
000049345 650_2 $$2MeSH$$aHydrogen-Ion Concentration
000049345 650_2 $$2MeSH$$aIons
000049345 650_2 $$2MeSH$$aKinetics
000049345 650_2 $$2MeSH$$aLight
000049345 650_2 $$2MeSH$$aModels, Chemical
000049345 650_2 $$2MeSH$$aMutation
000049345 650_2 $$2MeSH$$aPhotons
000049345 650_2 $$2MeSH$$aPhotoreceptor Cells, Invertebrate: chemistry
000049345 650_2 $$2MeSH$$aProtein Binding
000049345 650_2 $$2MeSH$$aProtein Structure, Tertiary
000049345 650_2 $$2MeSH$$aSerine: chemistry
000049345 650_2 $$2MeSH$$aSodium Chloride: pharmacology
000049345 650_2 $$2MeSH$$aSpectrophotometry
000049345 650_2 $$2MeSH$$aTemperature
000049345 650_2 $$2MeSH$$aTime Factors
000049345 650_7 $$00$$2NLM Chemicals$$aAnions
000049345 650_7 $$00$$2NLM Chemicals$$aCations
000049345 650_7 $$00$$2NLM Chemicals$$aCryptochromes
000049345 650_7 $$00$$2NLM Chemicals$$aDNA Adducts
000049345 650_7 $$00$$2NLM Chemicals$$aFlavoproteins
000049345 650_7 $$00$$2NLM Chemicals$$aIons
000049345 650_7 $$052-90-4$$2NLM Chemicals$$aCysteine
000049345 650_7 $$056-45-1$$2NLM Chemicals$$aSerine
000049345 650_7 $$07647-14-5$$2NLM Chemicals$$aSodium Chloride
000049345 650_7 $$2WoSType$$aJ
000049345 7001_ $$0P:(DE-Juel1)VDB16784$$aKottke, T.$$b1$$uFZJ
000049345 7001_ $$0P:(DE-HGF)0$$aHegemann, P.$$b2
000049345 7001_ $$0P:(DE-HGF)0$$aDick, B.$$b3
000049345 773__ $$0PERI:(DE-600)1477214-0$$a10.1529/biophysj.104.058230$$gVol. 89, p. 402 - 412$$p402 - 412$$q89<402 - 412$$tBiophysical journal$$v89$$x0006-3495$$y2005
000049345 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC1366540
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