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Updated: Aug 14, 2026

Local Field Fluorescence Microscopy: Imaging Cellular Signals in Intact Hearts
Published on: March 8, 2017
Adenosine diphosphate moiety does not participate in structural changes for the signaling state in the sensor of
Shinji Masuda1, Koji Hasegawa, Taka-Aki Ono
1Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama 226-5801, Japan. shmasuda@bio.titech.ac.jp
Abstract:
A sensor of blue light using FAD (BLUF) protein is a flavin adenine dinucleotide (FAD) based new class blue-light sensory flavoprotein. The BLUF domain of AppA was reconstituted in vitro from apoprotein and flavin adenine dinucleotide, flavin adenine mononucleotide or riboflavin. The light-induced FTIR spectra of the domain reconstituted from various flavins and the 13C-labeled apoprotein showed that identical light-induced structural changes occur in both the flavin chromophore and protein for the signaling state in all of the reconstituted holoproteins. The results showed that an adenosine 5'-dinucleotide moiety is not required for signaling-state formation in a BLUF domain.
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