PUBLICATION
Involvement of Electron Transfer in the Photoreaction of Zebrafish Cryptochrome-DASH
- Authors
- Zikihara, K., Ishikawa, T., Todo, T., and Tokutomi, S.
- ID
- ZDB-PUB-080527-12
- Date
- 2008
- Source
- Photochemistry and photobiology 84(4): 1016-1023 (Journal)
- Registered Authors
- Keywords
- none
- MeSH Terms
-
- Animals
- Cryptochromes
- Darkness
- Electron Transport*
- Flavoproteins/chemistry
- Flavoproteins/metabolism*
- Flavoproteins/radiation effects*
- Light
- Photoreceptor Cells/metabolism
- Spectrophotometry
- Zebrafish/metabolism*
- Zebrafish Proteins/chemistry
- Zebrafish Proteins/metabolism*
- Zebrafish Proteins/radiation effects*
- PubMed
- 18494763 Full text @ Photochem. Photobiol.
Citation
Zikihara, K., Ishikawa, T., Todo, T., and Tokutomi, S. (2008) Involvement of Electron Transfer in the Photoreaction of Zebrafish Cryptochrome-DASH. Photochemistry and photobiology. 84(4):1016-1023.
Abstract
Photoreaction of a blue-light photoreceptor Cryptochrome-DASH (Cry-DASH), a new member of the Cryptochrome family, from zebrafish was studied by UV-visible absorption spectroscopy in aqueous solutions at 293 K. Zebrafish Cry-DASH binds two chromophores, a flavin adenine dinucleotide (FAD) and a N5,N10-methenyl-5,6,7,8-tetrahydrofolate (MTHF) noncovalently. The bound FAD exists in the oxidized form (FAD(ox)) in the dark. Blue light converts FAD(ox) to the neutral radical form (FADH(*)). Formed FADH(*) is transformed to the fully reduced form FADH(2) (or FADH(-)) by successive light irradiation, or reverts to FAD(ox). FADH(2) (or FADH(-)) reverts to FADH(*) or possibly to FAD(ox) directly. The effect of dithiothreitol suggests a possible electron transfer between FAD in zebrafish Cry-DASH and reductants in the external medium. This is the first report on the photoreaction pathway and kinetics of a vertebrate Cry-DASH family protein.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping