ArticleJournal of the American Chemical Society2026
Protein Electrostatics Tune the Singlet-Triplet Energy Gap in Natural and Engineered Phototropin Light-Oxygen-Voltage (LOV) Domains.
Article in Journal of the American Chemical Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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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Who cites it
2 citing papers in PubMed.
- QM/MM Calculated Triplet-Singlet Infrared Difference Spectra of LOV2 Photoreceptor Domains and FMN in Solution.ACS omega · 2026Article
- Identification of Key Residues in Allosteric Signaling of Photoactivated Adenylyl Cyclase.bioRxiv : the preprint server for biology · 2026Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Photoactive flavoproteins such as Light-Oxygen-Voltage (LOV) domains serve as scaffolds for tuning the photophysics of their bound flavin cofactor through sequence mutations. This variable tuning effect has led to the development of a series of engineered LOV-based proteins that optimize fluorescence, intersystem crossing (ISC), photoreduction, and/or adduct formation over a range of time scales. To better guide future engineering efforts, we recently employed hybrid quantum mechanical/molecular mechanical (QM/MM) models of LOV domains to study how intradomain electrostatics exert control over flavin's photophysics. This work focuses on a series of three LOV1 and three LOV2 domains from
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Registered trials
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