ArticleThe Journal of biological chemistry2015
Proton transfer to flavin stabilizes the signaling state of the blue light receptor plant cryptochrome.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 63 citations in OpenAlex.
- Photochemistry of Receptor-Bound Flavin Resolved in Living Human Cells by Infrared Spectroscopy.Journal of the American Chemical Society · 2025Article
- Single Amino Acid Mutation Decouples Photochemistry of the BLUF Domain from the Enzymatic Function of OaPAC and Drives the Enzyme to a Switched-on State.Journal of molecular biology · 2024Article
- A structural decryption of cryptochromes.Frontiers in chemistry · 2024Review
- The cofactor-dependent folding mechanism of Drosophila cryptochrome revealed by single-molecule pulling experiments.Nature communications · 2023Article
- Insights into Molecular Structure of Pterins Suitable for Biomedical Applications.International journal of molecular sciences · 2022Review
- Unraveling the Photoactivation Mechanism of a Light-Activated Adenylyl Cyclase Using Ultrafast Spectroscopy Coupled with Unnatural Amino Acid Mutagenesis.ACS chemical biology · 2022Article
- Ultrafast photooxidation of protein-bound anionic flavin radicals.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The CRY2-COP1-HY5-BBX7/8 module regulates blue light-dependent cold acclimation in Arabidopsis.The Plant cell · 2021Article
- Cryptochromes: Photochemical and structural insight into magnetoreception.Protein science : a publication of the Protein Society · 2021Review
- Peripheral Methionine Residues Impact Flavin Photoreduction and Protonation in an Engineered LOV Domain Light Sensor.Biochemistry · 2021Article
- Structural insights into photoactivation of plant Cryptochrome-2.Communications biology · 2021Article
- Plant Cryptochromes Illuminated: A Spectroscopic Perspective on the Mechanism.Frontiers in chemistry · 2021Review
- Active-Site Environmental Factors Customize the Photophysics of Photoenzymatic Old Yellow Enzymes.The journal of physical chemistry. B · 2020Article
- Structural insights into BIC-mediated inactivation of Arabidopsis cryptochrome 2.Nature structural & molecular biology · 2020Article
- Physical methods for studying flavoprotein photoreceptors.Methods in enzymology · 2019Article
- Ion mobility action spectroscopy of flavin dianions reveals deprotomer-dependent photochemistry.Physical chemistry chemical physics : PCCP · 2018Article
- Electron transfer pathways in a light, oxygen, voltage (LOV) protein devoid of the photoactive cysteine.Scientific reports · 2017Article
- Hyperactivity of theThe Journal of biological chemistry · 2017Article
- Optogenetic activation of Plexin-B1 reveals contact repulsion between osteoclasts and osteoblasts.Nature communications · 2017Article
- Changes in active site histidine hydrogen bonding trigger cryptochrome activation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plant cryptochromes regulate the circadian rhythm, flowering time, and photomorphogenesis in higher plants as responses to blue light. In the dark, these photoreceptors bind oxidized FAD in the photolyase homology region (PHR). Upon blue light absorption, FAD is converted to the neutral radical state, the likely signaling state, by electron transfer via a conserved tryptophan triad and proton transfer from a nearby aspartic acid. Here we demonstrate, by infrared and time-resolved UV-visible spectroscopy on the PHR domain, that replacement of the aspartic acid Asp-396 with cysteine prevents proton transfer. The lifetime of the radical is decreased by 6 orders of magnitude. This short lifetime does not permit to drive conformational changes in the C-terminal extension that have been associated with signal transduction. Only in the presence of ATP do both the wild type and mutant form a long-lived radical state. However, in the mutant, an anion radical is formed instead of the neutral radical, as found previously in animal type I cryptochromes. Infrared spectroscopic experiments demonstrate that the light-induced conformational changes of the PHR domain are conserved in the mutant despite the lack of proton transfer. These changes are not detected in the photoreduction of the non-photosensory d-amino acid oxidase to the anion radical. In conclusion, formation of the anion radical is sufficient to generate a protein response in plant cryptochromes. Moreover, the intrinsic proton transfer is required for stabilization of the signaling state in the absence of ATP.
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