ArticleThe journal of physical chemistry. B2020
Active-Site Environmental Factors Customize the Photophysics of Photoenzymatic Old Yellow Enzymes.
Article in The journal of physical chemistry. B, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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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.
- Asymmetric Hydroamination Using Oxidative Radical Initiation in Flavin Enzymes.Journal of the American Chemical Society · 2026Article
- Ultrafast Photochemistry of Ligand-Bound Flavoprotein Amine Oxidases: Conformational Insights and Photocatalytic Implications.JACS Au · 2026Article
- Emergent Mechanisms in Biocatalysis.ACS central science · 2025Review
- Photoenzymatic Enantioselective Intermolecular Radical Hydroamination.Nature catalysis · 2023Article
- Tracking the Electron Transfer Cascade in European Robin Cryptochrome 4 Mutants.Journal of the American Chemical Society · 2023Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
The development of non-natural photoenzymatic systems has reinvigorated the study of photoinduced electron transfer (ET) within protein active sites, providing new and unique platforms for understanding how biological environments affect photochemical processes. In this work, we use ultrafast spectroscopy to compare the photoinduced electron transfer in known photoenzymes. 12-Oxophytodienoate reductase 1 (OPR1) is compared to Old Yellow Enzyme 1 (OYE1) and morphinone reductase (MR). The latter enzymes are structurally homologous to OPR1. We find that slight differences in the amino acid composition of the active sites of these proteins determine their distinct electron-transfer dynamics. Our work suggests that the inside of a protein active site is a complex/heterogeneous dielectric network where genetically programmed heterogeneity near the site of biological ET can significantly affect the presence and lifetime of various intermediate states. Our work motivates additional tunability of Old Yellow Enzyme active-site reorganization energy and electron-transfer energetics that could be leveraged for photoenzymatic redox approaches.
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Registered trials
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