ArticlePhotochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology2022
Comparing ultrafast excited state quenching of flavin 1,N
Article in Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- Direct Observation of Franck-Condon Stimulated Emission and Sub-20 fs Relaxation in Photoexcited Flavins.The journal of physical chemistry letters · 2026Article
- Photoinduced Electron Transfer Informs on Pathway Coupling in Flavin-Based Electron Bifurcation.ACS bio & med chem Au · 2026Article
- Electronic Structure Methods for Simulating Flavin's Spectroscopy and Photophysics: Comparison of Multi-reference, TD-DFT, and Single-Reference Wave Function Methods.The journal of physical chemistry. B · 2024Article
- Importance of Polarizable Embedding for Absorption Spectrum Calculations ofThe journal of physical chemistry. B · 2024Article
- Determining Excited-State Absorption Properties of a Quinoid Flavin by Polarization-Resolved Transient Spectroscopy.The journal of physical chemistry. A · 2024Article
Corrections and comments
- Erratum issued
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Flavins are photoenzymatic cofactors often exploiting the absorption of light to energize photoinduced redox chemistry in a variety of contexts. Both flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) are used for this function. The study of these photoenzymes has been facilitated using flavin analogs. Most of these analogs involve modification of the flavin ring, and there is recent evidence that adenine (Ade)-modified FAD can affect enzyme turnover, but so far this has only been shown for enzymes where the adenine and flavin rings are close to each other in a stacked conformation. FAD is also stacked in aqueous solution, and its photodynamics are quite different from unstacked FAD or FMN. Oxidized photoexcited FAD decays rapidly, presumably through PET with Ade as donor and Fl* as acceptor. Definitive identification of the spectral signatures of Ade
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Registered trials
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.