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| Home > Publications database > Functional variations among LOV domains as revealed by FTIR difference spectroscopy > print |
| 001 | 38378 | ||
| 005 | 20200402205641.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:15170487 |
| 024 | 7 | _ | |2 DOI |a 10.1039/b400976b |
| 024 | 7 | _ | |2 WOS |a WOS:000221746800012 |
| 037 | _ | _ | |a PreJuSER-38378 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 620 |
| 084 | _ | _ | |2 WoS |a Biochemistry & Molecular Biology |
| 084 | _ | _ | |2 WoS |a Biophysics |
| 084 | _ | _ | |2 WoS |a Chemistry, Physical |
| 100 | 1 | _ | |a Bednarz, T. |b 0 |u FZJ |0 P:(DE-Juel1)VDB37437 |
| 245 | _ | _ | |a Functional variations among LOV domains as revealed by FTIR difference spectroscopy |
| 260 | _ | _ | |a Cambridge |b Royal Society of Chemistry |c 2004 |
| 300 | _ | _ | |a 575 - 579 |
| 336 | 7 | _ | |a Journal Article |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a article |2 DRIVER |
| 440 | _ | 0 | |a Photochemical and Photobiological Sciences |x 1474-905X |0 9703 |v 3 |
| 500 | _ | _ | |a Record converted from VDB: 12.11.2012 |
| 520 | _ | _ | |a The two LOV domains, LOV1 and LOV2, from Chlamydomonas reinhardtii were investigated by light-induced FT-IR difference spectroscopy and compared to the LOV domain of Bacillus subtilis (YtvA-LOV). It is shown that the two S-H conformations of the reactive LOV1 cysteine C57(1) are exposed to environments of different hydrogen bonding strength. Thus, the two rotamer configurations of C57 might be related to the fact that the triplet state decays bi-exponentially into the LOV1-390 photoproduct. Exchange of the two other cysteines of LOV1 (C32S and C83S) does not alter the S-H stretching band providing evidence that this band feature arises solely from C57. The reactive cysteine of LOV2 from Chlamydomonas reinhardtii (C250) and of YtvA-LOV (C62) exhibit both a homogenous S-H stretching vibrational band which suggests a single conformer of the amino acid side chain. Finally, the FT-IR difference spectrum of YtvA from Bacillus subtilis comprising the light absorbing LOV domain and the putative signaling STAS (sulfate transporter/antisigma-factor antagonist) domain, reveals conformational changes in the latter after blue-light excitation. |
| 536 | _ | _ | |a Neurowissenschaften |c L01 |2 G:(DE-HGF) |0 G:(DE-Juel1)FUEK255 |x 0 |
| 588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
| 650 | _ | 2 | |2 MeSH |a Animals |
| 650 | _ | 2 | |2 MeSH |a Bacillus subtilis: physiology |
| 650 | _ | 2 | |2 MeSH |a Bacillus subtilis: radiation effects |
| 650 | _ | 2 | |2 MeSH |a Bacterial Proteins: chemistry |
| 650 | _ | 2 | |2 MeSH |a Bacterial Proteins: genetics |
| 650 | _ | 2 | |2 MeSH |a Bacterial Proteins: physiology |
| 650 | _ | 2 | |2 MeSH |a Chlamydomonas reinhardtii: physiology |
| 650 | _ | 2 | |2 MeSH |a Chlamydomonas reinhardtii: radiation effects |
| 650 | _ | 2 | |2 MeSH |a Crystallography, X-Ray |
| 650 | _ | 2 | |2 MeSH |a Protein Conformation |
| 650 | _ | 2 | |2 MeSH |a Spectrometry, Fluorescence |
| 650 | _ | 2 | |2 MeSH |a Spectroscopy, Fourier Transform Infrared: methods |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Bacterial Proteins |
| 650 | _ | 7 | |a J |2 WoSType |
| 700 | 1 | _ | |a Losi, A. |b 1 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Gärtner, W. |b 2 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Hegemann, P. |b 3 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Heberle, J. |b 4 |u FZJ |0 P:(DE-Juel1)VDB572 |
| 773 | _ | _ | |a 10.1039/b400976b |g Vol. 3, p. 575 - 579 |p 575 - 579 |q 3<575 - 579 |0 PERI:(DE-600)2072584-X |t Photochemical & photobiological sciences |v 3 |y 2004 |x 1474-905X |
| 856 | 7 | _ | |u http://dx.doi.org/10.1039/b400976b |
| 909 | C | O | |o oai:juser.fz-juelich.de:38378 |p VDB |
| 913 | 1 | _ | |k L01 |v Neurowissenschaften |l Funktion und Dysfunktion des Nervensystems |b Leben |0 G:(DE-Juel1)FUEK255 |x 0 |
| 914 | 1 | _ | |y 2004 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0010 |a JCR/ISI refereed |
| 920 | 1 | _ | |k IBI-2 |l Biologische Strukturforschung |d 31.12.2006 |g IBI |0 I:(DE-Juel1)VDB58 |x 0 |
| 970 | _ | _ | |a VDB:(DE-Juel1)49048 |
| 980 | _ | _ | |a VDB |
| 980 | _ | _ | |a ConvertedRecord |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a I:(DE-Juel1)ISB-2-20090406 |
| 980 | _ | _ | |a UNRESTRICTED |
| 980 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
| 981 | _ | _ | |a I:(DE-Juel1)IBI-7-20200312 |
| 981 | _ | _ | |a I:(DE-Juel1)ISB-2-20090406 |
| 981 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
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