000003640 001__ 3640
000003640 005__ 20200402205548.0
000003640 0247_ $$2pmid$$apmid:19217862
000003640 0247_ $$2pmc$$apmc:PMC2717236
000003640 0247_ $$2DOI$$a10.1016/j.bpj.2008.11.016
000003640 0247_ $$2WOS$$aWOS:000266377800021
000003640 037__ $$aPreJuSER-3640
000003640 041__ $$aeng
000003640 082__ $$a570
000003640 084__ $$2WoS$$aBiophysics
000003640 1001_ $$0P:(DE-Juel1)VDB58121$$aMajerus, T.$$b0$$uFZJ
000003640 245__ $$aTime-Resolved Fourier Transform Infrared Study on Photoadduct Formation and Secondary Structural Changes within the Phototropin LOV Domain
000003640 260__ $$aNew York, NY$$bRockefeller Univ. Press$$c2009
000003640 300__ $$a1462 - 1470
000003640 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
000003640 3367_ $$2DataCite$$aOutput Types/Journal article
000003640 3367_ $$00$$2EndNote$$aJournal Article
000003640 3367_ $$2BibTeX$$aARTICLE
000003640 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000003640 3367_ $$2DRIVER$$aarticle
000003640 440_0 $$0882$$aBiophysical Journal$$v96$$x0006-3495$$y4
000003640 500__ $$aThis work was Supported by the Helmholtz Genicinschaft (grant VHNG-014) and Deutsche Forschungsgemeinschaft (grant FOR 526).
000003640 520__ $$aPhototropins are plant blue-light photoreceptors containing two light-, oxygen-, or voltage-sensitive (LOV) domains and a C-terminal kinase domain. The two LOV domains bind noncovalently flavin mononucleotide as a chromophore. We investigated the photocycle of fast-recovery mutant LOV2-I403V from Arabidopsis phototropin 2 by step-scan Fourier transform infrared spectroscopy. The reaction of the triplet excited state of flavin with cysteine takes place with a time constant of 3 micros to yield the covalent adduct. Our data provide evidence that the flavin is unprotonated in the productive triplet state, disfavoring an ionic mechanism of bond formation. An intermediate adduct species was evident that displayed changes in secondary structure in the helix or loop region, and relaxed with a time constant of 120 micros. In milliseconds, the final adduct state is formed by further alterations of secondary structure, including beta-sheets. A comparison with wild-type adduct spectra shows that the mutation does not interfere with the functionality of the domain. All signals originate from within the LOV domain, because the construct does not comprise the adjacent Jalpha helix required for signal transduction. The contribution of early and late adduct intermediates to signal transfer to the Jalpha helix outside of the domain is discussed.
000003640 536__ $$0G:(DE-Juel1)FUEK307$$2G:(DE-HGF)$$aohne FE$$cohne FE$$x0
000003640 588__ $$aDataset connected to Web of Science, Pubmed
000003640 650_2 $$2MeSH$$aArabidopsis: chemistry
000003640 650_2 $$2MeSH$$aArabidopsis Proteins
000003640 650_2 $$2MeSH$$aCryptochromes
000003640 650_2 $$2MeSH$$aCysteine: chemistry
000003640 650_2 $$2MeSH$$aFlavoproteins: chemistry
000003640 650_2 $$2MeSH$$aFlavoproteins: genetics
000003640 650_2 $$2MeSH$$aKinetics
000003640 650_2 $$2MeSH$$aLasers
000003640 650_2 $$2MeSH$$aLight
000003640 650_2 $$2MeSH$$aModels, Molecular
000003640 650_2 $$2MeSH$$aMutation
000003640 650_2 $$2MeSH$$aProtein Structure, Secondary
000003640 650_2 $$2MeSH$$aProtein Structure, Tertiary
000003640 650_2 $$2MeSH$$aSpectroscopy, Fourier Transform Infrared
000003640 650_7 $$00$$2NLM Chemicals$$aArabidopsis Proteins
000003640 650_7 $$00$$2NLM Chemicals$$aCRY1 protein, Arabidopsis
000003640 650_7 $$00$$2NLM Chemicals$$aCryptochromes
000003640 650_7 $$00$$2NLM Chemicals$$aFlavoproteins
000003640 650_7 $$052-90-4$$2NLM Chemicals$$aCysteine
000003640 650_7 $$2WoSType$$aJ
000003640 7001_ $$0P:(DE-Juel1)VDB16784$$aKottke, T.$$b1$$uFZJ
000003640 773__ $$0PERI:(DE-600)1477214-0$$a10.1016/j.bpj.2008.11.016$$gVol. 96, p. 1462 - 1470$$p1462 - 1470$$q96<1462 - 1470$$tBiophysical journal$$v96$$x0006-3495$$y2009
000003640 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC2717236
000003640 909CO $$ooai:juser.fz-juelich.de:3640$$pVDB
000003640 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000003640 9141_ $$y2009
000003640 9131_ $$0G:(DE-Juel1)FUEK307$$aDE-HGF$$bohne FE$$kohne FE$$lohne FE$$vohne FE$$x0
000003640 9201_ $$0I:(DE-Juel1)ISB-2-20090406$$d31.12.2010$$gISB$$kISB-2$$lMolekulare Biophysik$$x0
000003640 970__ $$aVDB:(DE-Juel1)109879
000003640 980__ $$aVDB
000003640 980__ $$aConvertedRecord
000003640 980__ $$ajournal
000003640 980__ $$aI:(DE-Juel1)ICS-6-20110106
000003640 980__ $$aUNRESTRICTED
000003640 981__ $$aI:(DE-Juel1)IBI-7-20200312
000003640 981__ $$aI:(DE-Juel1)ICS-6-20110106
000003640 981__ $$aI:(DE-Juel1)ISB-2-20090406