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Updated: Mar 11, 2026

Novel Techniques for Observing Structural Dynamics of Photoresponsive Liquid Crystals
Published on: May 29, 2018
Light-induced structural changes of the LOV2 domains in various phototropins revealed by FTIR spectroscopy
Tatsuya Iwata1, Satoru Tokutomi2, Hideki Kandori3
1Center for Fostering Young and Innovative Researchers, Nagoya Institute of Technology, Showa-ku, Nagoya 466-8555, Japan; Department of Frontier Materials, Nagoya Institute of Technology, Showa-ku, Nagoya 466-8555, Japan.
Abstract:
Phototropin (Phot), a blue-light photoreceptor in plants, consists of two FMN-binding domains (named LOV1 and LOV2) and a serine/threonine (Ser/Thr) kinase domain. We have investigated light-induced structural changes of LOV domains, which lead to the activation of the kinase domain, by means of light-induced difference FTIR spectroscopy. FTIR spectroscopy revealed that the reactive cysteine is protonated in both unphotolyzed and triplet-excited states, which is difficult to detect by other methods such as X-ray crystallography. In this review, we describe the light-induced structural changes of hydrogen-bonding environment of FMN chromophore and protein backbone in Adiantum neo1-LOV2 in the C=O stretching region by use of 13C-labeled samples. We also describe the comprehensive FTIR analysis of LOV2 domains among Arabidopsis phot1, phot2, and Adiantum neo1 with and without Jα helix domain.
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