ArticleBiochemistry2011
Modulating LOV domain photodynamics with a residue alteration outside the chromophore binding site.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 55 citations in OpenAlex.
- Article
- Protein Electrostatics Tune the Singlet-Triplet Energy Gap in Natural and Engineered Phototropin Light-Oxygen-Voltage (LOV) Domains.Journal of the American Chemical Society · 2026Article
- Hydraulic Activation of the AsLOV2 Photoreceptor.bioRxiv : the preprint server for biology · 2025Article
- Structural dynamics of protein-protein association involved in the light-induced transition of Avena sativa LOV2 protein.Nature communications · 2024Article
- LOV1 protein of Pseudomonas cichorii JBC1 modulates its virulence and lifestyles in response to blue light.Scientific reports · 2024Article
- Triggered Functional Dynamics of AsLOV2 by Time-Resolved Electron Paramagnetic Resonance at High Magnetic Fields.Angewandte Chemie (International ed. in English) · 2023Article
- 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
- Photoinduced damage of AsLOV2 domain is accompanied by increased singlet oxygen production due to flavin dissociation.Scientific reports · 2020Article
- Directly light-regulated binding of RGS-LOV photoreceptors to anionic membrane phospholipids.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Bringing Light to Transcription: The Optogenetics Repertoire.Frontiers in genetics · 2018Review
- LOV-based optogenetic devices: light-driven modules to impart photoregulated control of cellular signaling.Frontiers in molecular biosciences · 2015Review
- Light-induced structural changes in a short light, oxygen, voltage (LOV) protein revealed by molecular dynamics simulations-implications for the understanding of LOV photoactivation.Frontiers in molecular biosciences · 2015Article
- Article
- Heterogeneous photodynamics of the pfr state in the cyanobacterial phytochrome Cph1.Biochemistry · 2014Article
- From Plant Infectivity to Growth Patterns: The Role of Blue-Light Sensing in the Prokaryotic World.Plants (Basel, Switzerland) · 2014Review
- Article
- Blue light-induced dimerization of a bacterial LOV-HTH DNA-binding protein.Biochemistry · 2013Article
- Signaling mechanisms of LOV domains: new insights from molecular dynamics studies.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2013Article
- Decrypting cryptochrome: revealing the molecular identity of the photoactivation reaction.Journal of the American Chemical Society · 2012Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Phototropins, a class of light-activated protein kinases, are essential for several blue light responses in plants and algae, including phototropism. These proteins contain two internal light, oxygen, and voltage sensitive (LOV) domains, which bind flavin chromophores and undergo a reversible photochemical formation of a cysteinyl-flavin adduct as part of the light sensing process. While the photodynamic properties of such photosensory domains are dictated by interactions between the chromophore and surrounding protein, more distant residues can play a significant role as well. Here we explore the role of the Phe434 residue in the photosensory response of the second LOV domain of Avena sativa phototropin 1 (AsLOV2), a model photochemical system for these LOV domains. Phe434 is more than 6 Å from the FMN chromophore in AsLOV2; nevertheless, an F434Y point mutation is likely to change several structural features of the chromophore binding site, as we demonstrate using molecular dynamics simulations. Transient absorption signals spanning 15 decades in time were compared for wild-type AsLOV2 and the F434Y mutant, showing that the latter has significantly altered photodynamics, including (i) a faster intersystem crossing leading to triplet formation on a nanosecond time scale, (ii) biphasic formation of adduct-state kinetics on the microsecond time scale, and (iii) greatly accelerated ground-state recovery kinetics on a second time scale. We present mechanistic models that link these spectroscopic differences to changes in the configuration of the critical cysteine residue and in the chromophore's accessibility to solvent and oxygen according to MD trajectories and purging experiments. Taken together, these results demonstrate the importance of residues outside the chromophore-binding pocket in modulating LOV domain photodynamics.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.