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 1.14.14.3 FMNH - 698992 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 FMNH2 8-substituted FMN-analogs 348586 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 FMNH2 enzyme is complexed with flavin mononucleotide, enzyme possesses a binding platform for the isoalloxazine ring of flavin, a chromophore whose 7,8-dimethyl benzene plane interacts with the isopropyl chain of alphaVal173, structure-fuction analysis 658060 1.14.14.3 FMNH2 physiological cofactor 658050 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 FMNH2 specific for, low activity with other flavins or flavin analogs 348585 1.14.14.3 iso-FMNH2 - 348574 1.14.14.3 additional information 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