ArticleJournal of the American Chemical Society2014
BLUF domain function does not require a metastable radical intermediate state.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 51 citations in OpenAlex.
- Identification of Key Residues in Allosteric Signaling of Photoactivated Adenylyl Cyclase.bioRxiv : the preprint server for biology · 2026Article
- Light-Driven Enzyme Catalysis: Ultrafast Mechanisms and Biochemical Implications.Biochemistry · 2025Review
- Probing the Signal Transduction Mechanism of the Light-Activated Adenylate Cyclase OaPAC Using Unnatural Amino Acid Mutagenesis.ACS chemical biology · 2025Article
- Enhancing Proton-Coupled Electron Transfer in Blue Light Using FAD Photoreceptor AppAJournal of the American Chemical Society · 2025Article
- Unveiling the Photoactivation Mechanism of BLUF Photoreceptor Protein through Hybrid Quantum Mechanics/Molecular Mechanics Free-Energy Calculation.ACS physical chemistry Au · 2024Article
- Article
- 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
- Origin of the multi-phasic quenching dynamics in the BLUF domains across the species.Nature communications · 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
- 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
- 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
- Photochemical processes in flavo-enzymes as a probe for active site dynamics: TrmFO of Thermus thermophilus.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2021Article
- Identification of the vibrational marker of tyrosine cation radical using ultrafast transient infrared spectroscopy of flavoprotein systems.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2021Article
- Photoreaction Mechanisms of Flavoprotein Photoreceptors and Their Applications.Advances in experimental medicine and biology · 2021Review
- 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
- Structural Basis for the Regulation of Biofilm Formation and Iron Uptake inACS infectious diseases · 2020Article
- Ultrafast Vibrational Energy Transfer between Protein and Cofactor in a Flavoenzyme.The journal of physical chemistry. B · 2020Article
- 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
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
BLUF (blue light using flavin) domain proteins are an important family of blue light-sensing proteins which control a wide variety of functions in cells. The primary light-activated step in the BLUF domain is not yet established. A number of experimental and theoretical studies points to a role for photoinduced electron transfer (PET) between a highly conserved tyrosine and the flavin chromophore to form a radical intermediate state. Here we investigate the role of PET in three different BLUF proteins, using ultrafast broadband transient infrared spectroscopy. We characterize and identify infrared active marker modes for excited and ground state species and use them to record photochemical dynamics in the proteins. We also generate mutants which unambiguously show PET and, through isotope labeling of the protein and the chromophore, are able to assign modes characteristic of both flavin and protein radical states. We find that these radical intermediates are not observed in two of the three BLUF domains studied, casting doubt on the importance of the formation of a population of radical intermediates in the BLUF photocycle. Further, unnatural amino acid mutagenesis is used to replace the conserved tyrosine with fluorotyrosines, thus modifying the driving force for the proposed electron transfer reaction; the rate changes observed are also not consistent with a PET mechanism. Thus, while intermediates of PET reactions can be observed in BLUF proteins they are not correlated with photoactivity, suggesting that radical intermediates are not central to their operation. Alternative nonradical pathways including a keto-enol tautomerization induced by electronic excitation of the flavin ring are considered.
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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.