EC Number   |
Cofactor  |
Reference |
|---|
   1.14.14.3 | 1-deaza-FMNH2 |
can replace FMNH2 |
348552 |
| 1.14.14.3 | 2',3'-Diacetyl-FMNH2 |
as substitute for FMNH2 |
348574 |
| 1.14.14.3 | 2-Thio-FMNH2 |
as substitute for FMNH2 |
348574 |
| 1.14.14.3 | 3-carboxymethyl-FMNH2 |
as substitute for FMNH2 |
348574 |
| 1.14.14.3 | 4a-hydroxy-4a,5-dihydroriboflavin-5'-phosphate |
model bioluminescence emitter molecule, binding and fluorescence quantum yield studies, complexed with the enzyme in a 1:1 molcular ratio |
658050 |
| 1.14.14.3 | FMN |
- |
702318, 704579 |
| 1.14.14.3 | FMN |
dependent on |
727031 |
| 1.14.14.3 | FMN |
potassium iodide quenches the fluorescence of FMN |
676321 |
| 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 |
702699 |
| 1.14.14.3 | FMN |
the luminescence reaction is initiated by the reduction of FMN |
702496 |
