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Literature summary extracted from

  • Vetrova, E.V.; Kudryasheva, N.S.; Cheng, K.H.
    Effect of quinone on the fluorescence decay dynamics of endogenous flavin bound to bacterial luciferase (2009), Biophys. Chem., 141, 59-65.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.14.3 1,4-benzoquinone
-
Photobacterium leiognathi
1.14.14.3 2-methyl-1,4-benzoquinone
-
Photobacterium leiognathi
1.14.14.3 2-methyl-5-isopropyl-1,4-benzoquinone
-
Photobacterium leiognathi
1.14.14.3 additional information hydrophobicity of the quinone plays a role in the non-specific inhibition mechanism of xenobiotic molecules in the bacterial bioluminescence system via altering the rotational mobility of the endogenous flavin in the luciferase. Added quinone reduces the averaged binding affinity of the endogenous FMN to the active site of luciferase by increasing the fraction of the weak FMN binding sites of luciferase Photobacterium leiognathi

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.3 Photobacterium leiognathi
-
-
-

Storage Stability

EC Number Storage Stability Organism
1.14.14.3 -20°C Photobacterium leiognathi

Synonyms

EC Number Synonyms Comment Organism
1.14.14.3 bacterial luciferase
-
Photobacterium leiognathi

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.3 FMN presence of two discrete and well-separated intensity decay lifetimes (ca. 1 and 5 ns) and intensity decay heterogeneity, of the neat sample suggests that the endogenous FMN senses a heterogeneous fluorescence quenching microenvironment at the active site of the luciferase. Free FMN in solution (isotropic environment), exhibits a single decay lifetime (5 ns), i.e., no intensity decay heterogeneity. Intensity decay heterogeneity of endogenous FMN is largely preserved in the presence of quinone. Averaged rotational rate of FMN increases with the increasing hydrophobicity of the quinone Photobacterium leiognathi