Alternative links to fulltext:
| Item type: | Article | ||||
|---|---|---|---|---|---|
| Journal or Publication Title: | ChemBioChem | ||||
| Volume: | 8 | ||||
| Number of Issue or Book Chapter: | 18 | ||||
| Page Range: | pp. 2256-2264 | ||||
| Date: | 2007 | ||||
| Additional Information (public): | CAN 148:489258 6-3 General Biochemistry 146-17-8 (FMN) Role: BSU (Biological study, unclassified), PEP (Physical, engineering or chemical process), PRP (Properties), BIOL (Biological study), PROC (Process) (chem. vs. photochem. redn. and influence on photocycle in relation to redox properties of photocycle LOV1 domain and FMN) | ||||
| Institutions: | Chemistry and Pharmacy > Institut für Physikalische und Theoretische Chemie > Chair of Chemistry III - Physical Chemistry (Molecular Spectroscopy and Photochemistry) > Prof. Dr. Bernhard Dick | ||||
| Identification Number: |
| ||||
| Keywords: | Protein motifs (LOV1 (light-oxygen-voltage-sensitive 1) domain, chem. vs. photochem. redn. and influence on photocycle in relation to redox properties of photocycle LOV1 domain and FMN); Chlamydomonas reinhardtii; Redox potential; Reduction; Reduction, photochemical (chem. vs. photochem. redn. and influence on photocycle in relation to redox properties of photocycle LOV1 domain and FMN); Phototropins Role: BSU (Biological study, unclassified), PEP (Physical, engineering or chemical process), PRP (Properties), BIOL (Biological study), PROC (Process) (chem. vs. photochem. redn. and influence on photocycle in relation to redox properties of photocycle LOV1 domain and FMN); phototropin LOV domain FMN redox photochem redn | ||||
| 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: | 5570 |
Abstract
LOV (light-oxygen-voltage-sensitive) domains comprise the light-sensitive parts of many blue light photoreceptor proteins. Photo-excitation of the chromophore FMN in these LOV domains leads to formation of a covalent adduct between FMN and a cysteine residue. So far, the electronically excited singlet and triplet states of FMN have been identified as the only intermediates in the photocycles of ...
Abstract
LOV (light-oxygen-voltage-sensitive) domains comprise the light-sensitive parts of many blue light photoreceptor proteins. Photo-excitation of the chromophore FMN in these LOV domains leads to formation of a covalent adduct between FMN and a cysteine residue. So far, the electronically excited singlet and triplet states of FMN have been identified as the only intermediates in the photocycles of LOV domains from several organisms. Since many flavoproteins are redox-active, however, the photocycles of LOV domains might involve other redox states of FMN, and might be controlled by the external redox potential. Here we report on the redox properties of the LOV1 domain from phototropin of the green alga Chlamydomonas reinhardtii. By equil.-redox spectropotentiometry a redox potential [Efq/fhq (flavoquinone/flavohydroquinone)] of -290 mV vs. the normal hydrogen electrode (NHE) was detd. for the wild-type domain (LOV1-wt). A similar value of -280 mV was found for the mutant LOV1-C57G, in which the photoreactive cysteine is replaced by glycine. The recovery kinetics (photoadduct->ground state) in the photocycle of LOV1-wt are not influenced by a redox potential in the range between +500 and -260 mV vs. NHE. No flavosemiquinone could be generated by chem. redn. with sodium dithionite. However, photoredn. of LOV1-C57G with EDTA leads exclusively to the flavosemiquinone. This semiquinone is stable against disproportionation, and the photoredn. is not mediated by free FMN.
Metadata last modified: 24 May 2018 10:11
Owner only: item control page
Altmetric