ArticleBiophysical journal2009
Time-resolved Fourier transform infrared study on photoadduct formation and secondary structural changes within the phototropin LOV domain.
Article in Biophysical journal, 2009. 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.
- QM/MM Calculated Triplet-Singlet Infrared Difference Spectra of LOV2 Photoreceptor Domains and FMN in Solution.ACS omega · 2026Article
- Regulation of Conidiation and Aflatoxin B1 Biosynthesis by a Blue Light Sensor LreA inJournal of fungi (Basel, Switzerland) · 2024Article
- Article
- Review
- Signal transduction in light-oxygen-voltage receptors lacking the active-site glutamine.Nature communications · 2022Article
- QM calculations predict the energetics and infrared spectra of transient glutamine isomers in LOV photoreceptors.Physical chemistry chemical physics : PCCP · 2021Article
- Peripheral Methionine Residues Impact Flavin Photoreduction and Protonation in an Engineered LOV Domain Light Sensor.Biochemistry · 2021Article
- Engineering Photosensory Modules of Non-Opsin-Based Optogenetic Actuators.International journal of molecular sciences · 2020Review
- Signal transduction in photoreceptor histidine kinases.Protein science : a publication of the Protein Society · 2019Review
- Helical Contributions Mediate Light-Activated Conformational Change in the LOV2 Domain ofACS omega · 2019Article
- Light sensing and responses in fungi.Nature reviews. Microbiology · 2019Review
- Variation in LOV Photoreceptor Activation Dynamics Probed by Time-Resolved Infrared Spectroscopy.Biochemistry · 2018Article
- Sequential conformational transitions and α-helical supercoiling regulate a sensor histidine kinase.Nature communications · 2017Article
- Glutamine Amide Flip Elicits Long Distance Allosteric Responses in the LOV Protein Vivid.Journal of the American Chemical Society · 2017Article
- Femtosecond to Millisecond Dynamics of Light Induced Allostery in the Avena sativa LOV Domain.The journal of physical chemistry. B · 2017Article
- Signal transduction in light-oxygen-voltage receptors lacking the adduct-forming cysteine residue.Nature communications · 2015Article
- Photochemistry of flavoprotein light sensors.Nature chemical biology · 2014Review
- A dominant mutation in the light-oxygen and voltage2 domain vicinity impairs phototropin1 signaling in tomato.Plant physiology · 2014Article
- Aureochrome 1 illuminated: structural changes of a transcription factor probed by molecular spectroscopy.PloS one · 2014Article
- Mechanism of signal transduction of the LOV2-Jα photosensor from Avena sativa.Nature communications · 2010Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phototropins are plant blue-light photoreceptors containing two light-, oxygen-, or voltage-sensitive (LOV) domains and a C-terminal kinase domain. The two LOV domains bind noncovalently flavin mononucleotide as a chromophore. We investigated the photocycle of fast-recovery mutant LOV2-I403V from Arabidopsis phototropin 2 by step-scan Fourier transform infrared spectroscopy. The reaction of the triplet excited state of flavin with cysteine takes place with a time constant of 3 micros to yield the covalent adduct. Our data provide evidence that the flavin is unprotonated in the productive triplet state, disfavoring an ionic mechanism of bond formation. An intermediate adduct species was evident that displayed changes in secondary structure in the helix or loop region, and relaxed with a time constant of 120 micros. In milliseconds, the final adduct state is formed by further alterations of secondary structure, including beta-sheets. A comparison with wild-type adduct spectra shows that the mutation does not interfere with the functionality of the domain. All signals originate from within the LOV domain, because the construct does not comprise the adjacent Jalpha helix required for signal transduction. The contribution of early and late adduct intermediates to signal transfer to the Jalpha helix outside of the domain is discussed.
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