title: Dinoflagellate luminescence: purification of a NAD(P)H-dependent reductase and of its substrate.
abstract: The soluble enzymatic luminescent system of the dinoflagellate Pyrocystis lunula (luciferase-luciferin) is coupled with an enzymatic NAD(P)H-dependent reaction. The enzyme is a soluble reductase (Mr 47,000) which catalyzes, in the presence of NAD(P)H, the reduction of a molecule called P630. Reduced P630 has the same spectral characteristics as the purified luciferin. The luciferase can oxidize this reduced molecule with a light emission at 480 nm. These observations suggest that reduced P630 is a luciferin molecule. The oxidized form seems, in these conditions, to be the precursor of luciferin.
mesh_terms: D000818:Animals; D004141:Dinoflagellida / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008156:Luciferases / Q000378:metabolism; D008163:Luminescent Measurements; D009243:NAD / Q000494:pharmacology; D009247:NADH, NADPH Oxidoreductases / Q000302:isolation & purification* / Q000378:metabolism; D009249:NADP / Q000494:pharmacology; D013057:Spectrum Analysis / Q000379:methods; D013379:Substrate Specificity
chemical_list: D009243:NAD; D009249:NADP; D008156:Luciferases; D009247:NADH, NADPH Oxidoreductases