ArticleThe Journal of biological chemistry2012
Redox modulation of flavin and tyrosine determines photoinduced proton-coupled electron transfer and photoactivation of BLUF photoreceptors.
Article in The Journal of biological chemistry, 2012. 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.
- 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
- Enhancing Proton-Coupled Electron Transfer in Blue Light Using FAD Photoreceptor AppAJournal of the American Chemical Society · 2025Article
- Spectroscopic and Computational Observation of Glutamine Tautomerization in the Blue Light Sensing Using Flavin Domain Photoreaction.Journal of the American Chemical Society · 2023Article
- Tuning the redox potential of tyrosine-histidine bioinspired assemblies.Photosynthesis research · 2022Article
- 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
- Excited State Vibrations of Isotopically Labeled FMN Free and Bound to a Light-Oxygen-Voltage (LOV) Protein.The journal of physical chemistry. B · 2020Article
- A Robust Bioderived Wavelength-Specific Photosensor Based on BLUF Proteins.Sensors and actuators. B, Chemical · 2020Article
- Proton-coupled electron transfer across benzimidazole bridges in bioinspired proton wires.Chemical science · 2020Article
- Tuning Radical Relay Residues by Proton Management Rescues Protein Electron Hopping.Journal of the American Chemical Society · 2019Article
- Constructing Molecular π-Orbital Active Spaces for Multireference Calculations of Conjugated Systems.Journal of chemical theory and computation · 2019Article
- Physical methods for studying flavoprotein photoreceptors.Methods in enzymology · 2019Article
- Flavin Conjugated Polydopamine Nanoparticles Displaying Light-Driven Monooxygenase Activity.Frontiers in chemistry · 2019Article
- BlsA Is a Low to Moderate Temperature Blue Light Photoreceptor in the Human PathogenFrontiers in microbiology · 2019Article
- Light-induced chromophore and protein responses and mechanical signal transduction of BLUF proteins.Biophysical reviews · 2018Review
- Distinct properties underlie flavin-based electron bifurcation in a novel electron transfer flavoprotein FixAB fromThe Journal of biological chemistry · 2018Article
- Photoactivation of the BLUF Protein PixD Probed by the Site-Specific Incorporation of Fluorotyrosine Residues.Journal of the American Chemical Society · 2017Article
- Equilibrium and ultrafast kinetic studies manipulating electron transfer: A short-lived flavin semiquinone is not sufficient for electron bifurcation.The Journal of biological chemistry · 2017Article
- 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
- A proposal for a dipole-generated BLUF domain mechanism.Frontiers in molecular biosciences · 2015Article
- Biochemistry and theory of proton-coupled electron transfer.Chemical reviews · 2014Review
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Authors and funding
4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Photoinduced electron transfer in biological systems, especially in proteins, is a highly intriguing matter. Its mechanistic details cannot be addressed by structural data obtained by crystallography alone because this provides only static information on a given redox system. In combination with transient spectroscopy and site-directed manipulation of the protein, however, a dynamic molecular picture of the ET process may be obtained. In BLUF (blue light sensors using FAD) photoreceptors, proton-coupled electron transfer between a tyrosine and the flavin cofactor is the key reaction to switch from a dark-adapted to a light-adapted state, which corresponds to the biological signaling state. Particularly puzzling is the fact that, although the various naturally occurring BLUF domains show little difference in the amino acid composition of the flavin binding pocket, the reaction rates of the forward reaction differ quite largely from a few ps up to several hundred ps. In this study, we modified the redox potential of the flavin/tyrosine redox pair by site-directed mutagenesis close to the flavin C2 carbonyl and fluorination of the tyrosine, respectively. We provide information on how changes in the redox potential of either reaction partner significantly influence photoinduced proton-coupled electron transfer. The altered redox potentials allowed us furthermore to experimentally describe an excited state charge transfer intermediately prior to electron transfer in the BLUF photocycle. Additionally, we show that the electron transfer rate directly correlates with the quantum yield of signaling state formation.
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