Publisher Summary This chapter focuses on the application of Renilla bioluminescence system including the characteristics of the proteins and substrates involved in the light-emitting process. The molecular basis for Renilla bioluminescence, as well as certain features of its nerve-linked control are also described. The requirement for 3´,5´-diphosphoadenosine (PAP) in Renilla bioluminescence involved a cofactor in the conversion of luciferyl sulfate to coelenterate-type luciferin by the enzyme luciferin sulfokinase. The assay for PAP involves a coupled-enzyme luminescence assay utilizing luciferyl sulfate as the substrate. Renilla luciferase is purified to homogeneity from crude extracts with an overall recovery of 24%. Luciferase also contains three free SH groups but no disulfide linkages. Renilla luciferase can be classified as an oxygenase (O 2 ) as it is apparently incorporated into one of the products, oxyluciferin, while a second product, carbon dioxide (CO 2 ) is derived from carbon 3 of luciferin. The initial product of the reaction is an electronic excited state of luciferaseoxyluciferin-monoanion complex that relaxes to its ground state with the production of blue light.
Renilla Luciferase Free SH Groups Disulfide Linkages Conversion Of Sulfate Crude Extracts Production Of Light Carbon Dioxide Ground State Application Of System Free Groups
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Climate change Research Articles published between Nov 14, 2022 to Nov 20, 2022
Nov 21, 2022
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