ArticleBiophysical journal2008
Hydrogen bond switching among flavin and amino acid side chains in the BLUF photoreceptor observed by ultrafast infrared spectroscopy.
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 33 papers.
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Who cites it
33 citing papers in PubMed, 104 citations in OpenAlex.
- Enhancing Proton-Coupled Electron Transfer in Blue Light Using FAD Photoreceptor AppAJournal of the American Chemical Society · 2025Article
- Single Amino Acid Mutation Decouples Photochemistry of the BLUF Domain from the Enzymatic Function of OaPAC and Drives the Enzyme to a Switched-on State.Journal of molecular biology · 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
- Photoinduced Electron Transfer from a 1,4,5,6-Tetrahydro Nicotinamide Adenine Dinucleotide (Phosphate) Analogue to Oxidized Flavin in an Ene-Reductase Flavoenzyme.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
- Optophysiology: Illuminating cell physiology with optogenetics.Physiological reviews · 2022Review
- 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
- Optobiochemistry: Genetically Encoded Control of Protein Activity by Light.Annual review of biochemistry · 2021Review
- Light-Driven Enzymatic Decarboxylation of Dicarboxylic Acids.ChemistryOpen · 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
- Ultrafast flavin/tryptophan radical pair kinetics in a magnetically sensitive artificial protein.Physical chemistry chemical physics : PCCP · 2019Article
- Constructing Molecular π-Orbital Active Spaces for Multireference Calculations of Conjugated Systems.Journal of chemical theory and computation · 2019Article
- Hydrocarbon Synthesis via Photoenzymatic Decarboxylation of Carboxylic Acids.Journal of the American Chemical Society · 2019Article
- Physical methods for studying flavoprotein photoreceptors.Methods in enzymology · 2019Article
- Ion mobility action spectroscopy of flavin dianions reveals deprotomer-dependent photochemistry.Physical chemistry chemical physics : PCCP · 2018Article
- 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
- Role of active site conformational changes in photocycle activation of the AppA BLUF photoreceptor.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- A proposal for a dipole-generated BLUF domain mechanism.Frontiers in molecular biosciences · 2015Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
BLUF domains constitute a recently discovered class of photoreceptor proteins found in bacteria and eukaryotic algae. BLUF domains are blue-light sensitive through a FAD cofactor that is involved in an extensive hydrogen-bond network with nearby amino acid side chains, including a highly conserved tyrosine and glutamine. The participation of particular amino acid side chains in the ultrafast hydrogen-bond switching reaction with FAD that underlies photoactivation of BLUF domains is assessed by means of ultrafast infrared spectroscopy. Blue-light absorption by FAD results in formation of FAD(*-) and a bleach of the tyrosine ring vibrational mode on a picosecond timescale, showing that electron transfer from tyrosine to FAD constitutes the primary photochemistry. This interpretation is supported by the absence of a kinetic isotope effect on the fluorescence decay on H/D exchange. Subsequent protonation of FAD(*-) to result in FADH(*) on a picosecond timescale is evidenced by the appearance of a N-H bending mode at the FAD N5 protonation site and of a FADH(*) C=N stretch marker mode, with tyrosine as the likely proton donor. FADH(*) is reoxidized in 67 ps (180 ps in D(2)O) to result in a long-lived hydrogen-bond switched network around FAD. This hydrogen-bond switch shows infrared signatures from the C-OH stretch of tyrosine and the FAD C4=O and C=N stretches, which indicate increased hydrogen-bond strength at all these sites. The results support a previously hypothesized rotation of glutamine by approximately 180 degrees through a light-driven radical-pair mechanism as the determinant of the hydrogen-bond switch.
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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.