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