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Literature summary for 1.14.14.3 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
Search for more literature for 1.14.14.3

Inhibitors

Inhibitors Comment Organism Structure
1,4-benzoquinone
-
 Photobacterium leiognathi
2-methyl-1,4-benzoquinone
-
 Photobacterium leiognathi
2-methyl-5-isopropyl-1,4-benzoquinone
-
 Photobacterium leiognathi
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

Organism UniProt Comment Textmining
Photobacterium leiognathi
-
-
-

Storage Stability

Storage Stability Organism
-20°C Photobacterium leiognathi

Synonyms

Synonyms Comment Organism
bacterial luciferase
-
 Photobacterium leiognathi

Cofactor

Cofactor Comment Organism Structure
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