Literature DB >> 21405544

Structural change of a cofactor binding site of flavoprotein detected by single-protein fluorescence spectroscopy at 1.5 k.

Satoru Fujiyoshi1, Mitsuharu Hirano, Michio Matsushita, Mineo Iseki, Masakatsu Watanabe.   

Abstract

The visible fluorescence spectrum of single flavoprotein at a temperature of 1.5 K has been measured by one-photon excitation. The flavoprotein studied was a photoswitchable enzyme, photoactivated adenylyl cyclase. The time course of the spectrum revealed a structural change occurring at a rate of 10(-3)  s(-1) around hydrogen bonds at the flavin cofactor binding site.

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Year:  2011        PMID: 21405544     DOI: 10.1103/PhysRevLett.106.078101

Source DB:  PubMed          Journal:  Phys Rev Lett        ISSN: 0031-9007            Impact factor:   9.161


  2 in total

1.  Photoactivated Adenylyl Cyclases: Fundamental Properties and Applications.

Authors:  Mineo Iseki; Sam-Yong Park
Journal:  Adv Exp Med Biol       Date:  2021       Impact factor: 2.622

2.  Reflecting microscope system with a 0.99 numerical aperture designed for three-dimensional fluorescence imaging of individual molecules at cryogenic temperatures.

Authors:  H Inagawa; Y Toratani; K Motohashi; I Nakamura; M Matsushita; S Fujiyoshi
Journal:  Sci Rep       Date:  2015-08-04       Impact factor: 4.379

  2 in total

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