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| Item type: | Article | ||||
|---|---|---|---|---|---|
| Journal or Publication Title: | ChemBioChem | ||||
| Volume: | 9 | ||||
| Number of Issue or Book Chapter: | 6 | ||||
| Page Range: | pp. 861-864 | ||||
| Date: | 2008 | ||||
| Additional Information (public): | 6-3 General Biochemistry 52-90-4 (L-Cysteine) Role: BSU (Biological study, unclassified), BIOL (Biological study) (LOV1 protein from Chlamydomonas reinhardtii is a template for photoadduct formation of FMN and Me mercaptan); 74-93-1 (Methyl mercaptan); 146-17-8 (FMN) Role: BSU (Biological study, unclassified), RCT (Reactant), BIOL (Biological study), RACT (Reactant or reagent) (LOV1 protein from Chlamydomonas reinhardtii is a template for photoadduct formation of FMN and Me mercaptan) | ||||
| 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, Blaulicht-sensitive Photorezeptoren | ||||
| Identification Number: |
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| Keywords: | Chlamydomonas reinhardtii (LOV1 protein from Chlamydomonas reinhardtii is a template for photoadduct formation of FMN and Me mercaptan); Phototropins; Role: BSU (Biological study, unclassified), BIOL (Biological study) (LOV1 protein from Chlamydomonas reinhardtii is a template for photoadduct formation of FMN and Me mercaptan); Protein motifs (LOV1, LOV1 protein from Chlamydomonas reinhardtii is a template for photoadduct formation of FMN and Me mercaptan); Proteins, Role: BSU (Biological study, unclassified), RCT (Reactant), BIOL (Biological study), RACT (Reactant or reagent) (light oxygen voltage sensitive (LOV) protein domain-contg., LOV1 protein from Chlamydomonas reinhardtii is a template for photoadduct formation of FMN and Me mercaptan); LOV1 protein FMN methyl mercaptan adduct cysteine phototropin | ||||
| 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: | 5563 |
Abstract
The adduct of FMN and methylmercaptane was synthesized inside the binding pocket of a light oxygen voltage sensitive (LOV) protein domain in which the cysteine residue of the wild type has been replaced by the photochem. inactive amino acid glycine. In the absence of the protein, the photoreaction between FMN and MM yields the fully reduced hydroquinone form FMNH2 or the anion FMNH. The reaction ...
Abstract
The adduct of FMN and methylmercaptane was synthesized inside the binding pocket of a light oxygen voltage sensitive (LOV) protein domain in which the cysteine residue of the wild type has been replaced by the photochem. inactive amino acid glycine. In the absence of the protein, the photoreaction between FMN and MM yields the fully reduced hydroquinone form FMNH2 or the anion FMNH. The reaction mechanism of the synthesized FMN and MM adduct is briefly described. The adduct postulated by us is a flavin deriv. with a thioalkyl residue at the C4a-position and a hydrogen atom at the N5-position. It is readily hydrolyzed either by protonation at the sulfur atom or by deprotonation at N5. However, it can be formed and stabilized for many hours in the flavin binding pocket of a LOV protein domain. Thus, the protein not only plays a decisive role in guiding the reaction towards this product, but also in keeping it stable. It is assumed that the reaction proceeds along the same mechanism as the cysteine adduct formation in the wild-type protein, albeit with lower quantum yields and rate consts.
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