ArticleScientific reports2017
Electron transfer pathways in a light, oxygen, voltage (LOV) protein devoid of the photoactive cysteine.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 70 citations in OpenAlex.
- Toward Relative Redox Potential Predictions in Flavoproteins: Treatment of a Charge-Changing Mutation in Alchemical Free Energy Simulations.Journal of chemical theory and computation · 2026Article
- Flowering time regulation: a critical review focusing on FKF1 protein.Plant molecular biology · 2026Review
- Article
- Small Protein Domains as Potential Spin Labels for In Vitro, Cellular, and Light-Induced Dipolar EPR Spectroscopy.Journal of the American Chemical Society · 2025Article
- Flavoproteins as native and genetically encoded spin probes for in cell ESR spectroscopy.Nature communications · 2025Article
- Light-dependent flavin redox and adduct states control the conformation and DNA-binding activity of the transcription factor EL222.Nucleic acids research · 2025Article
- Light reception of Phycomyces revisited: several white collar proteins confer blue- and red-light sensitivity and control dynamic range and adaptation.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2024Review
- LOV1 protein of Pseudomonas cichorii JBC1 modulates its virulence and lifestyles in response to blue light.Scientific reports · 2024Article
- Reduction midpoint potential of a paradigm light-oxygen-voltage receptor and its modulation by methionine residues.RSC chemical biology · 2024Article
- Triggered Functional Dynamics of AsLOV2 by Time-Resolved Electron Paramagnetic Resonance at High Magnetic Fields.Angewandte Chemie (International ed. in English) · 2023Article
- Enzymatic Spin-Labeling of Protein N- and C-Termini for Electron Paramagnetic Resonance Spectroscopy.Bioconjugate chemistry · 2023Article
- Sub-Millisecond Photoinduced Dynamics of Free and EL222-Bound FMN by Stimulated Raman and Visible Absorption Spectroscopies.Biomolecules · 2023Article
- 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
- A light life together: photosensing in the plant microbiota.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2021Review
- Computational Investigation of Structural and Spectroscopic Properties of LOV-Based Proteins with Improved Fluorescence.The journal of physical chemistry. B · 2021Article
- Tailored flavoproteins acting as light-driven spin machines pump nuclear hyperpolarization.Scientific reports · 2020Article
- Unraveling the Mechanism of a LOV Domain Optogenetic Sensor: A Glutamine Lever Induces Unfolding of the Jα Helix.ACS chemical biology · 2020Article
- Light-Mediated Decreases in Cyclic di-GMP Levels Inhibit Structure Formation inJournal of bacteriology · 2020Article
Corrections and comments
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Authors and funding
10 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Blue-light absorption by the flavin chromophore in light, oxygen, voltage (LOV) photoreceptors triggers photochemical reactions that lead to the formation of a flavin-cysteine adduct. While it has long been assumed that adduct formation is essential for signaling, it was recently shown that LOV photoreceptor variants devoid of the photoactive cysteine can elicit a functional response and that flavin photoreduction to the neutral semiquinone radical is sufficient for signal transduction. Currently, the mechanistic basis of the underlying electron- (eT) and proton-transfer (pT) reactions is not well understood. We here reengineered pT into the naturally not photoreducible iLOV protein, a fluorescent reporter protein derived from the Arabidopsis thaliana phototropin-2 LOV2 domain. A single amino-acid substitution (Q489D) enabled efficient photoreduction, suggesting that an eT pathway is naturally present in the protein. By using a combination of site-directed mutagenesis, steady-state UV/Vis, transient absorption and electron paramagnetic resonance spectroscopy, we investigate the underlying eT and pT reactions. Our study provides strong evidence that several Tyr and Trp residues, highly conserved in all LOV proteins, constitute the eT pathway for flavin photoreduction, suggesting that the propensity for photoreduction is evolutionary imprinted in all LOV domains, while efficient pT is needed to stabilize the neutral semiquinone radical.
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