Spectroscopic investigations of the single tryptophan residue and of riboflavin and 7-oxolumazine bound to lumazine apoprotein from Photobacterium leiognathi.

@article{Kulinski1987SpectroscopicIO,
  title={Spectroscopic investigations of the single tryptophan residue and of riboflavin and 7-oxolumazine bound to lumazine apoprotein from Photobacterium leiognathi.},
  author={Tadeusz Kulinski and Antonie J.W.G. Visser and Dennis J. O'Kane and J Lee},
  journal={Biochemistry},
  year={1987},
  volume={26 2},
  pages={
          540-9
        }
}
Spectroscopic techniques have been applied to investigate the conformation, local structure, and dynamic properties of the apoprotein of the lumazine protein from Photobacterium leiognathi and the holoprotein reconstituted with either the natural ligand 6,7-dimethyl-8-ribityllumazine or the closely related analogues riboflavin and 6-methyl-7-oxo-8-ribityllumazine (7-oxolumazine). The analogues are bound similarly to the natural prosthetic group. They exhibit similar shifts on binding in their… 
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Properties of recombinant fluorescent proteins from Photobacterium leiognathi and their interaction with luciferase intermediates.
TLDR
Fluorescence emission anisotropy decay was used to establish that none of these holoproteins complexed with native luciferase and that the lumazine protein alone formed a 1:1 complex with theLuciferase hydroxyflavin fluorescent transient and the Luciferase peroxyflavin intermediates.
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