Ataka, K. and Hegemann, Peter and Heberle, J. (2003) Vibrational spectroscopy of an algal Phot-LOV1 domain probes the molecular changes associated with blue-light reception. BIOPHYSICAL JOURNAL, 84 (1). pp. 466-474. ISSN 0006-3495
Full text not available from this repository.Abstract
The LOV1 domain of the blue light Phot1-receptor (phototropin homolog) from Chlamydomonas reinhardtii has been studied by vibrational spectroscopy. The FMN modes of the dark state of LOV1 were identified by preresonance Raman spectroscopy and assigned to molecular vibrations. By comparing the blue-light-induced FTIR difference spectrum, with the preresonance Raman spectrum, most of the differences are due to FMN modes. Thus, we exclude large backbone changes, of the protein that might occur during the phototransformation of the dark state LOV1-447 into the putative signaling state LOV1-390. Still, the presence of smaller amide difference bands cannot be excluded but may be masked by overlapping FMN modes. The band at 2567 cm(-1) is assigned to the S-H stretching vibration of C57, the residue that forms the transient thio-adduct with, the chromophore FMN. The occurrence of this band is evidence that C57 is protonated in the dark state of LOV1. This result challenges conclusions from the homologous LOV2 domain from oat that the thiolate of the corresponding cysteine is the, reactive species.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PLANT PHOTORECEPTOR DOMAIN; FLAVIN MONONUCLEOTIDE; CHLAMYDOMONAS-REINHARDTII; RAMAN-SPECTROSCOPY; LOV2 DOMAIN; SIDE-CHAINS; PROTEIN; PHOTOTROPIN; FLAVOPROTEINS; CHROMOPHORE; |
| 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: | 25 Aug 2021 10:51 |
| Last Modified: | 25 Aug 2021 10:51 |
| URI: | https://pred.uni-regensburg.de/id/eprint/39404 |
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