ArticleThe journal of physical chemistry letters2014
Dynamic Determination of Active-Site Reactivity in Semiquinone Photolyase by the Cofactor Photoreduction.
Article in The journal of physical chemistry letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed.
- Electron Transport through a Tryptophan Quadruplex in a Dimeric Azurin Construct.The journal of physical chemistry. B · 2026Article
- Tryptophan to Tryptophan Hole Hopping in an Azurin Construct.The journal of physical chemistry. B · 2024Article
- Active-Site Environmental Factors Customize the Photophysics of Photoenzymatic Old Yellow Enzymes.The journal of physical chemistry. B · 2020Article
- Understanding Short-Range Electron-Transfer Dynamics in Proteins.The journal of physical chemistry letters · 2019Article
- Short-Range Electron Transfer in Reduced Flavodoxin: Ultrafast Nonequilibrium Dynamics Coupled with Protein Fluctuations.The journal of physical chemistry letters · 2018Article
- Photolyase: Dynamics and electron-transfer mechanisms of DNA repair.Archives of biochemistry and biophysics · 2017Review
- Photolyase: Dynamics and Mechanisms of Repair of Sun-Induced DNA Damage.Photochemistry and photobiology · 2017Review
- Direct determination of resonance energy transfer in photolyase: structural alignment for the functional state.The journal of physical chemistry. A · 2014Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Photolyase contains a flavin cofactor in a fully reduced form as its functional state to repair ultraviolet-damaged DNA upon blue light absorption. However, after purification, the cofactor exists in its oxidized or neutral semiquinone state. Such oxidization eliminates the repair function, but it can be reverted by photoreduction, a photoinduced process with a series of electron-transfer (ET) reactions. With femtosecond absorption spectroscopy and site-directed mutagenesis, we completely recharacterized such photoreduction dynamics in the semiquinone state. Comparing with all previous studies, we identified a new intramolecular ET pathway, determined stretched ET behaviors, refined all ET time scales, and finally evaluated the driving forces and reorganization energies for eight elementary ET reactions. Combined with the oxidized-state photoreduction dynamics, we elucidated the different active-site properties of the reduction ability and structural flexibility in the oxidized and semiquinone states, leading to the dramatically different ET dynamics and photoreduction efficiency in the two states.
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Registered trials
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