EC Number   |
Cofactor |
Reference  |
|---|
   1.14.14.3 | FMNH2 |
- |
348552, 348579, 657751, 657855, 657923, 657927, 657939, 657994, 658147, 658495, 671414, 671610, 671978, 671985, 676010, 698992, 711341 |
| 1.14.14.3 | FMN |
potassium iodide quenches the fluorescence of FMN |
676321 |
| 1.14.14.3 | more |
the 4a-hydroperoxy-4a,5-dihydroFMN intermediate luciferase transforms from a low quantum yield IIx to a high quantum yield IIy fluorescent species on exposure to excitation light |
676321 |
| 1.14.14.3 | FMNH2 |
reduced FMN, i.e. FMNH2, generated by several species of flavin reductases, is utilized along with a long-chain aliphatic aldehyde and molecular oxygen by luciferase as substrates for the bioluminescence reaction, direct transfer of reduced flavin cofactor and reduced flavin product of reductase to luciferase, overview |
689388 |
| 1.14.14.3 | FMNH |
- |
698992 |
| 1.14.14.3 | FMN |
the luminescence reaction is initiated by the reduction of FMN |
702496 |
| 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 |
- |
702318, 704579 |
| 1.14.14.3 | FMNH2 |
binds to a mobile loop of 29 amino acids in the luciferase protein, structure and conformation, overview |
711486 |
| 1.14.14.3 | FMN |
dependent on |
727031 |
