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Updated: Feb 17, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
Variation in LOV Photoreceptor Activation Dynamics Probed by Time-Resolved Infrared Spectroscopy
James N Iuliano1, Agnieszka A Gil1, Sergey P Laptenok2
1Department of Chemistry, Stony Brook University , Stony Brook, New York 11794, United States.
Light-oxygen-voltage (LOV) proteins use flavin mononucleotide (FMN) for blue light sensing. This study reveals conserved FMN adduct formation but divergent downstream signaling in LOV photoreceptors, crucial for optogenetics.
Area of Science:
- Biochemistry
- Photobiology
- Molecular Biology
Background:
- Light-oxygen-voltage (LOV) domains are blue light sensors utilizing flavin mononucleotide (FMN).
- Their modularity enables applications in optogenetics and optobiology through fusion to output domains.
- Understanding LOV domain dynamics is key to designing novel light-controlled systems.
Purpose of the Study:
- To investigate the ultrafast to microsecond dynamics of three full-length LOV domain photoreceptors.
- To compare the conserved FMN adduct formation pathway with variable signaling kinetics.
- To link spectral and kinetic differences to specific output functions of LOV domains.
Main Methods:
- Transient infrared spectroscopy was employed to study LOV-STAS (YtvA), LOV-HTH (EL222), and LOV-histidine kinase (LovK).
- Spectroscopic analysis covered timescales from subpicoseconds to hundreds of microseconds.
- Kinetic and vibrational spectral changes post-adduct formation were analyzed.
Main Results:
- A conserved pathway for cysteine adduct formation from the FMN triplet state was observed across all tested LOV proteins.
- Slight variations in the rate of adduct formation were noted.
- Significant differences in post-adduct vibrational spectra and kinetics were found, correlating with distinct output domains.
Conclusions:
- The initial light-induced signaling cascade involving FMN adduct formation is highly conserved in LOV photoreceptors.
- Subsequent large-scale structural changes and signaling kinetics vary significantly (orders of magnitude) based on the specific output domain.
- These findings provide insights into the structure-function relationships of LOV-based optogenetic tools.
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