ArticleBiophysical journal2008
Molecular models predict light-induced glutamine tautomerization in BLUF photoreceptors.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed.
- Probing the Signal Transduction Mechanism of the Light-Activated Adenylate Cyclase OaPAC Using Unnatural Amino Acid Mutagenesis.ACS chemical biology · 2025Article
- Unveiling the Photoactivation Mechanism of BLUF Photoreceptor Protein through Hybrid Quantum Mechanics/Molecular Mechanics Free-Energy Calculation.ACS physical chemistry Au · 2024Article
- How Aqueous Solvation Impacts the Frequencies and Intensities of Infrared Absorption Bands in Flavin: The Quest for a Suitable Solvent Model.Molecules (Basel, Switzerland) · 2024Article
- Integrated Computational Study of the Light-Activated Structure of the AppA BLUF Domain and Its Spectral Signatures.The journal of physical chemistry. A · 2023Article
- Exploring Proton-Coupled Electron Transfer at Multiple Scales.Nature computational science · 2023Article
- Fast Method for Excited-State Dynamics in Complex Systems and Its Application to the Photoactivation of a Blue Light Using Flavin Photoreceptor.The journal of physical chemistry letters · 2023Article
- Spectroscopic and Computational Observation of Glutamine Tautomerization in the Blue Light Sensing Using Flavin Domain Photoreaction.Journal of the American Chemical Society · 2023Article
- Unraveling the Photoactivation Mechanism of a Light-Activated Adenylyl Cyclase Using Ultrafast Spectroscopy Coupled with Unnatural Amino Acid Mutagenesis.ACS chemical 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
- From crystallographic data to the solution structure of photoreceptors: the case of the AppA BLUF domain.Chemical science · 2021Article
- QM calculations predict the energetics and infrared spectra of transient glutamine isomers in LOV photoreceptors.Physical chemistry chemical physics : PCCP · 2021Article
- Formation of an unusual glutamine tautomer in a blue light using flavin photocycle characterizes the light-adapted state.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Physical methods for studying flavoprotein photoreceptors.Methods in enzymology · 2019Article
- Blue-Light Receptors for Optogenetics.Chemical reviews · 2018Review
- Light-induced chromophore and protein responses and mechanical signal transduction of BLUF proteins.Biophysical reviews · 2018Review
- Photoactivation of the BLUF Protein PixD Probed by the Site-Specific Incorporation of Fluorotyrosine Residues.Journal of the American Chemical Society · 2017Article
- Molecular mechanism of photoactivation of a light-regulated adenylate cyclase.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Femtosecond to Millisecond Dynamics of Light Induced Allostery in the Avena sativa LOV Domain.The journal of physical chemistry. B · 2017Article
- Evidence for Tautomerisation of Glutamine in BLUF Blue Light Receptors by Vibrational Spectroscopy and Computational Chemistry.Scientific reports · 2016Article
- Mechanism of the AppABLUF Photocycle Probed by Site-Specific Incorporation of Fluorotyrosine Residues: Effect of the Y21 pKa on the Forward and Reverse Ground-State Reactions.Journal of the American Chemical Society · 2016Article
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4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The recently discovered photoreceptor proteins containing BLUF (sensor of blue light using FAD) domains mediate physiological responses to blue light in bacteria and euglena. In BLUF domains, blue light activates the flavin chromophore yielding a signaling state characterized by a approximately 10 nm red-shifted absorption. We developed molecular models for the dark and light states of the BLUF domain of the Rhodobacter sphaeroides AppA protein, which are based on the crystal structures and quantum-mechanical simulations. According to these models, photon absorption by the flavin results in a tautomerization and 180 degree rotation of the Gln side chain that interacts with the flavin cofactor. This chemical modification of the Gln residue induces alterations in the hydrogen bond network in the core of the photoreceptor domain, which were observed in numerous spectroscopic experiments. The calculated electronic transition energies and vibrational frequencies of the proposed dark and light states are consistent with the optical and IR spectral changes observed during the photocycle. Light-induced isomerization of an amino acid residue instead of a chromophore represents a feature that has not been described previously in photoreceptors.
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