Fluorescence depolarization measurements of flavin mononucleotide embedded in the Light-Oxygen-Voltage (LOV) domain of the protein phototropin may be analyzed to detect the formation and/or dissociation of LOV homodimers. This study was conducted to determine whether fluorescence anisotropy decay could be used in identifying the formation or dissociation of dimers in the LOV domains from Rhodobacter sphaeroides and Chlamydomonas reinhardtii, respectively. Time-correlated single photon counting techniques were employed to measure the fluorescence anisotropy of the dark-state recovery of excited samples of LOV protein. Fluorescence anisotropy decay of FMN within the LOV domains appears to be a sufficient method in detection of dimer formation and dissociation. We expect this information will be helpful in understanding signal transduction in phototropin from Rhodobacter sphaeroides and Chlamydomonas reinhardtii.

Fluorescence anisotropy decay of FMN in LOV domains from Rhodobacter sphaeroides and Chlamydomonas reinhardtii

253rd National Meeting (2017)

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