ArticleProceedings of the National Academy of Sciences of the United States of America2013
Determining complete electron flow in the cofactor photoreduction of oxidized photolyase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed.
- Electron Transport through a Tryptophan Quadruplex in a Dimeric Azurin Construct.The journal of physical chemistry. B · 2026Article
- Design of Light Driven Hole Bifurcating Proteins.ACS central science · 2025Article
- Decrypting the Nonadiabatic Photoinduced Electron Transfer Mechanism in Light-Sensing Cryptochrome.ACS central science · 2025Article
- Redox-State-Dependent Structural Changes within a Prokaryotic 6-4 Photolyase.Journal of the American Chemical Society · 2025Article
- Elucidation of a distinct photoreduction pathway in class IIProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Dynamics and mechanism of DNA repair by a bifunctional cryptochrome.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Directed ultrafast conformational changes accompany electron transfer in a photolyase as resolved by serial crystallography.Nature chemistry · 2024Article
- Tryptophan to Tryptophan Hole Hopping in an Azurin Construct.The journal of physical chemistry. B · 2024Article
- Tracking the Electron Transfer Cascade in European Robin Cryptochrome 4 Mutants.Journal of the American Chemical Society · 2023Article
- Electrochemical and Structural Study of the Buried Tryptophan in Azurin: Effects of Hydration and Polarity on the Redox Potential of W48.The journal of physical chemistry. B · 2023Article
- Ultrafast Dynamics and Catalytic Mechanism of Fatty Acid Photodecarboxylase.Angewandte Chemie (International ed. in English) · 2022Article
- Serial crystallography captures dynamic control of sequential electron and proton transfer events in a flavoenzyme.Nature chemistry · 2022Article
- Insights into the Thermodynamics and Kinetics of Amino-Acid Radicals in Proteins.Annual review of biophysics · 2022Review
- Concerted and Stepwise Proton-Coupled Electron Transfer for Tryptophan-Derivative Oxidation with Water as the Primary Proton Acceptor: Clarifying a Controversy.Journal of the American Chemical Society · 2022Article
- Limited solvation of an electron donating tryptophan stabilizes a photoinduced charge-separated state in plant (6-4) photolyase.Scientific reports · 2022Article
- Dynamics and mechanism of dimer dissociation of photoreceptor UVR8.Nature communications · 2022Article
- Functional and protective hole hopping in metalloenzymes.Chemical science · 2021Review
- Ultrafast photoreduction dynamics of a new class of CPD photolyases.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2021Article
- Peripheral Methionine Residues Impact Flavin Photoreduction and Protonation in an Engineered LOV Domain Light Sensor.Biochemistry · 2021Article
- Photoinduced hole hopping through tryptophans in proteins.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
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7 authors.
Funding
Abstract
The flavin cofactor in photoenzyme photolyase and photoreceptor cryptochrome may exist in an oxidized state and should be converted into reduced state(s) for biological functions. Such redox changes can be efficiently achieved by photoinduced electron transfer (ET) through a series of aromatic residues in the enzyme. Here, we report our complete characterization of photoreduction dynamics of photolyase with femtosecond resolution. With various site-directed mutations, we identified all possible electron donors in the enzyme and determined their ET timescales. The excited cofactor behaves as an electron sink to draw electron flow from a series of encircling aromatic molecules in three distinct layers from the active site in the center to the protein surface. The dominant electron flow follows the conserved tryptophan triad in a hopping pathway across the layers with multiple tunneling steps. These ET dynamics occur ultrafast in less than 150 ps and are strongly coupled with local protein and solvent relaxations. The reverse electron flow from the flavin is slow and in the nanosecond range to ensure high reduction efficiency. With 12 experimentally determined elementary ET steps and 6 ET reaction pairs, the enzyme exhibits a distinct reduction-potential gradient along the same aromatic residues with favorable reorganization energies to drive a highly unidirectional electron flow toward the active-site center from the protein surface.
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