ArticleThe journal of physical chemistry. A2014
Direct determination of resonance energy transfer in photolyase: structural alignment for the functional state.
Article in The journal of physical chemistry. A, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Light-Driven Enzyme Catalysis: Ultrafast Mechanisms and Biochemical Implications.Biochemistry · 2025Review
- All Light, Everywhere? Photoreceptors at Nonconventional Sites.Physiology (Bethesda, Md.) · 2024Review
- A deazariboflavin chromophore kinetically stabilizes reduced FAD state in a bifunctional cryptochrome.Scientific reports · 2023Article
- Insights into Molecular Structure of Pterins Suitable for Biomedical Applications.International journal of molecular sciences · 2022Review
- Enhanced DNA repair by DNA photolyase bearing an artificial light-harvesting chromophore.Nucleic acids research · 2020Article
- Photolyase: Dynamics and Mechanisms of Repair of Sun-Induced DNA Damage.Photochemistry and photobiology · 2017Review
- Characterization of the Intermediate in and Identification of the Repair Mechanism of (6-4) Photolesions by Photolyases.Angewandte Chemie (International ed. in English) · 2016Article
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Authors and funding
8 authors.
Funding
Abstract
Photoantenna is essential to energy transduction in photoinduced biological machinery. A photoenzyme, photolyase, has a light-harvesting pigment of methenyltetrahydrofolate (MTHF) that transfers its excitation energy to the catalytic flavin cofactor FADH¯ to enhance DNA-repair efficiency. Here we report our systematic characterization and direct determination of the ultrafast dynamics of resonance energy transfer from excited MTHF to three flavin redox states in E. coli photolyase by capturing the intermediates formed through the energy transfer and thus excluding the electron-transfer quenching pathway. We observed 170 ps for excitation energy transferring to the fully reduced hydroquinone FADH¯, 20 ps to the fully oxidized FAD, and 18 ps to the neutral semiquinone FADH(•), and the corresponding orientation factors (κ(2)) were determined to be 2.84, 1.53 and 1.26, respectively, perfectly matching with our calculated theoretical values. Thus, under physiological conditions and over the course of evolution, photolyase has adopted the optimized orientation of its photopigment to efficiently convert solar energy for repair of damaged DNA.
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