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| Dokumentenart: | Artikel | ||||
|---|---|---|---|---|---|
| Titel eines Journals oder einer Zeitschrift: | Biophysical Journal | ||||
| Band: | 84 | ||||
| Nummer des Zeitschriftenheftes oder des Kapitels: | 2, Pt. | ||||
| Seitenbereich: | S. 1192-1201 | ||||
| Datum: | 2003 | ||||
| Zusätzliche Informationen (Öffentlich): | 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) | ||||
| Institutionen: | Chemie und Pharmazie > Institut für Physikalische und Theoretische Chemie > Chair of Chemistry III - Physical Chemistry (Molecular Spectroscopy and Photochemistry) > Prof. Dr. Bernhard Dick | ||||
| Sonstige Projekte: | GRK 640 Sensory photoreceptors in natural and artificial systems | ||||
| Identifikationsnummer: |
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| Stichwörter / 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-Dezimal-Klassifikation: | 500 Naturwissenschaften und Mathematik > 570 Biowissenschaften, Biologie 500 Naturwissenschaften und Mathematik > 540 Chemie | ||||
| Status: | Veröffentlicht | ||||
| Begutachtet: | Ja, diese Version wurde begutachtet | ||||
| An der Universität Regensburg entstanden: | Ja | ||||
| Dokumenten-ID: | 5561 |
Zusammenfassung
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 ...
Zusammenfassung
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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