Bednarz, T. and Losi, A. and Gaertner, W. and Hegemann, P. and Heberle, J. (2004) Functional variations among LOV domains as revealed by FT-IR difference spectroscopy. PHOTOCHEMICAL & PHOTOBIOLOGICAL SCIENCES, 3 (6). pp. 575-579. ISSN 1474-905X, 1474-9092
Full text not available from this repository.Abstract
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 biexponentially 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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | BLUE-LIGHT RECEPTOR; ALGA CHLAMYDOMONAS-REINHARDTII; PLANT PHOTORECEPTOR DOMAIN; S-H BAND; ADIANTUM PHYTOCHROME3; STRUCTURAL-CHANGES; PHOT-LOV1 DOMAIN; BINDING DOMAINS; PHOTOTROPIN; PHOTOCYCLE; |
| Subjects: | 500 Science > 540 Chemistry & allied sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Biochemie I |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 27 Jul 2021 08:01 |
| Last Modified: | 27 Jul 2021 08:01 |
| URI: | https://pred.uni-regensburg.de/id/eprint/38240 |
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