ArticleThe Journal of biological chemistry2016
Essential Role of an Unusually Long-lived Tyrosyl Radical in the Response to Red Light of the Animal-like Cryptochrome aCRY.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 63 citations in OpenAlex.
- Conserved structural motifs in PAS, LOV, and CRY proteins regulate circadian rhythms and are therapeutic targets.FEBS letters · 2026Review
- Capturing structural intermediates in an animal-like cryptochrome photoreceptor by time-resolved crystallography.Science advances · 2025Article
- Dynamics and mechanism of DNA repair by a bifunctional cryptochrome.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- A structural decryption of cryptochromes.Frontiers in chemistry · 2024Review
- A marine cryptochrome with an inverse photo-oligomerization mechanism.Nature communications · 2023Article
- A deazariboflavin chromophore kinetically stabilizes reduced FAD state in a bifunctional cryptochrome.Scientific reports · 2023Article
- Tryptophan Can Promote Oxygen Reduction to Water in a Biosynthetic Model of Heme Copper Oxidases.Biochemistry · 2023Article
- Direct experimental observation of blue-light-induced conformational change and intermolecular interactions of cryptochrome.Communications biology · 2022Article
- The nature of proton-coupled electron transfer in a blue light using flavin domain.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Cryptochrome magnetoreception: four tryptophans could be better than three.Journal of the Royal Society, Interface · 2021Article
- Cryptochromes: Photochemical and structural insight into magnetoreception.Protein science : a publication of the Protein Society · 2021Review
- Tuning flavin environment to detect and control light-induced conformational switching in Drosophila cryptochrome.Communications biology · 2021Article
- Plant Cryptochromes Illuminated: A Spectroscopic Perspective on the Mechanism.Frontiers in chemistry · 2021Review
- The World of Algae Reveals a Broad Variety of Cryptochrome Properties and Functions.Frontiers in plant science · 2021Review
- A Case Study of Eukaryogenesis: The Evolution of Photoreception by Photolyase/Cryptochrome Proteins.Journal of molecular evolution · 2020Article
- Chemical and structural analysis of a photoactive vertebrate cryptochrome from pigeon.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Time-Resolved Infrared and Visible Spectroscopy on Cryptochrome aCRY: Basis for Red Light Reception.Biophysical journal · 2019Article
- Structural changes within the bifunctional cryptochrome/photolyase CraCRY upon blue light excitation.Scientific reports · 2019Article
- Ultrafast flavin/tryptophan radical pair kinetics in a magnetically sensitive artificial protein.Physical chemistry chemical physics : PCCP · 2019Article
- The sacrificial inactivation of the blue-light photosensor cryptochrome from Drosophila melanogaster.Physical chemistry chemical physics : PCCP · 2018Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cryptochromes constitute a group of flavin-binding blue light receptors in bacteria, fungi, plants, and insects. Recently, the response of cryptochromes to light was extended to nearly the entire visible spectral region on the basis of the activity of the animal-like cryptochrome aCRY in the green alga Chlamydomonas reinhardtii This finding was explained by the absorption of red light by the flavin neutral radical as the dark state of the receptor, which then forms the anionic fully reduced state. In this study, time-resolved UV-visible spectroscopy on the full-length aCRY revealed an unusually long-lived tyrosyl radical with a lifetime of 2.6 s, which is present already 1 μs after red light illumination of the flavin radical. Mutational studies disclosed the tyrosine 373 close to the surface to form the long-lived radical and to be essential for photoreduction. This residue is conserved exclusively in the sequences of other putative aCRY proteins distinguishing them from conventional (6-4) photolyases. Size exclusion chromatography showed the full-length aCRY to be a dimer in the dark at 0.5 mm injected concentration with the C-terminal extension as the dimerization site. Upon illumination, partial oligomerization was observed via disulfide bridge formation at cysteine 482 in close proximity to tyrosine 373. The lack of any light response in the C-terminal extension as evidenced by FTIR spectroscopy differentiates aCRY from plant and Drosophila cryptochromes. These findings imply that aCRY might have evolved a different signaling mechanism via a light-triggered redox cascade culminating in photooxidation of a yet unknown substrate or binding partner.
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