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| Item type: | Article | ||||
|---|---|---|---|---|---|
| Journal or Publication Title: | Biophysical Journal | ||||
| Volume: | 84 | ||||
| Number of Issue or Book Chapter: | 2, Pt. | ||||
| Page Range: | pp. 1192-1201 | ||||
| Date: | 2003 | ||||
| Additional Information (public): | CAN 138:299473 6-3 General Biochemistry 52-90-4 (L-Cysteine) Role: BSU (Biological study, unclassified), BIOL (Biological study) (57, thiol adduct formation by; photocycle of a blue-light receptor domain LOV1 of Phot1 photoreceptor from Chlamydomonas reinhardtii); 146-17-8 (FMN) Role: BSU (Biological study, unclassified), BIOL (Biological study) (photocycle of a blue-light receptor domain LOV1 of Phot1 photoreceptor from Chlamydomonas reinhardtii) | ||||
| Institutions: | Chemistry and Pharmacy > Institut für Physikalische und Theoretische Chemie > Chair of Chemistry III - Physical Chemistry (Molecular Spectroscopy and Photochemistry) > Prof. Dr. Bernhard Dick | ||||
| Projects: | GRK 640 Sensory photoreceptors in natural and artificial systems | ||||
| Identification Number: |
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| Keywords: | Protein motifs (LOV1 domain, photocycle of a blue-light receptor domain LOV1 of Phot1 photoreceptor from Chlamydomonas reinhardtii); Photoreceptors, Role: BSU (Biological study, unclassified), PRP (Properties), BIOL (Biological study) (Phot1, LOV1 domain of, photocycle of a blue-light receptor domain LOV1 of Phot1 photoreceptor from Chlamydomonas reinhardtii); Chlamydomonas reinhardtii; Light; Photochemistry; Photoexcitation; Signal transduction; Triplet state (photocycle of a blue-light receptor domain LOV1 of Phot1 photoreceptor from Chlamydomonas reinhardtii); photoreceptor Phot1 LOV1 domain photocycle Chlamydomonas reinhardtii | ||||
| Dewey Decimal Classification: | 500 Science > 570 Life sciences 500 Science > 540 Chemistry & allied sciences | ||||
| Status: | Published | ||||
| Refereed: | Yes, this version has been refereed | ||||
| Created at the University of Regensburg: | Yes | ||||
| Item ID: | 5561 |
Abstract
The \"Phot\" protein family comprises blue-light photoreceptors that consist of two FMN-binding LOV (light, oxygen, and voltage) domains and a serine/threonine kinase domain. We have investigated the LOV1 domain of Phot1 from Chlamydomonas reinhardtii by time-resolved absorption spectroscopy. Photoexcitation of the dark form, LOV1-447, causes transient bleaching and formation of two spectrally ...
Abstract
The Phot
protein family comprises blue-light photoreceptors that consist of two FMN-binding LOV (light, oxygen, and voltage) domains and a serine/threonine kinase domain. We have investigated the LOV1 domain of Phot1 from Chlamydomonas reinhardtii by time-resolved absorption spectroscopy. Photoexcitation of the dark form, LOV1-447, causes transient bleaching and formation of two spectrally similar red-shifted intermediates that are both assigned to triplet states of the FMN. The triplet states decay with time consts. of 800 ns and 4 ms with an efficiency of >90% into a blue-shifted intermediate, LOV1-390, that is attributed to a thiol adduct of cysteine 57 to FMN C(4a). LOV1-390 reverts to the dark form in hundreds of seconds, the time const. being dependent on pH and salt concn. In the mutant C57S, where the thiol adduct cannot be formed, the triplet state displays an oxygen-dependent decay directly to the dark form. We present here a spectroscopic characterization of an algal sensory photoreceptor in general and of a LOV1 domain photocycle in particular. The results are discussed with respect to the behavior of the homologous LOV2 domain from oat.
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