Metal-ion mediated interaction of luciferase with tetraiodofluorescein.
Tetraiodofluorescein binds to luciferase in an apparently competitive manner, according to kinetic inactivation studies. Among the metal ions studied, Cu2+ and Ni2+ are the only two of the first row transition series that enhance enzyme inactivation by the dye. Mg2+, Co2+ and Mn2+ seem to have a protective effect whereas Zn2+ prevents enzyme inactivation and even enhances its activity. Luciferase bound to tetraiodofluorescien-Sepharose via a metal ion can subsequently be eluted with appropriate ligands. Luciferase was found to be sensitive to the spacer geometry of immobilized tetraiodofluorescein.
D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D002847:Chromatography, Agarose; D004923:Erythrosine / Q000378:metabolism / Q000494:pharmacology*; D005452:Fluoresceins / Q000494:pharmacology*; D007313:Insecta / Q000201:enzymology; D007700:Kinetics; D008156:Luciferases / Q000037:antagonists & inhibitors* / Q000378:metabolism; D011485:Protein Binding; D013997:Time Factors
D005452:Fluoresceins; D008156:Luciferases; D004923:Erythrosine