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The results presented here provide evidence that it is feasible to monitor two distinct activities at 37 degrees C with these novel thermostable proteins. Light emission from the North American firefly Photinus pyralis, which emits yellow-green nm light, is widely believed to be the most efficient bioluminescence system known, making this luciferase an excellent tool for monitoring gene expression. These results suggest that the novel enzymes should provide superior performance in dual-color reporter and in vivo imaging applications, and they illustrate the importance of codon optimization for assays in mammalian cells. We present studies on the production of a set of thermostable red- and green-emitting luciferase mutants with bioluminescent properties suitable for dual-color reporter assays, biosensor measurements with internal controls, and imaging techniques. The novel enzymes were expressed in HEK cells, where they performed similarly to Promega's codon-optimized click beetle red luciferase in model reporter assays. Model studies established that the luciferases could be detected at the attomole level and six orders of magnitude higher. North American firefly Photinus pyralis luciferase, which emits yellow-green light nm , has been adapted for a variety of applications, including gene reporter assays, whole-cell biosensor measurements, and in vivo imaging.
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Luciferine – Wikipedia

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On binding coelenterazine, oxygen spontaneously adds to form the photoprotein-bound substrate, the 2-hydroperoxycoelenterazine top right. August um The question to answer then is: The GFP's occurring in bioluminescent organisms all have fluorescence maxima in the range only nm.
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The longest spectral maximum is nm, a yellow bioluminescence found in a single strain of Alliivibrio sifiae previously called Vibrio fischeri , strain Y1 Figure In some way that has not been yet determined, luciferase amino acid residues are recruited to promote the addition of molecular oxygen to the D-luciferin adenylate, which is then transformed to an electronically excited state oxyluciferin molecule and carbon dioxide, each containing one oxygen atom from molecular oxygen. Photochem Photobiol Sci Crystal structure shows that the trans structure of the keto-oxy-Luciferin is the most stable form see Naumov et al.
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The results presented here provide evidence that it is feasible to monitor two distinct activities at 37 degrees C with these novel thermostable proteins. The novel enzymes were expressed in HEK cells, where they performed similarly to Promega's codon-optimized click beetle red luciferase in model reporter assays. Luciferase variants with red-shifted bioluminescence and high specific activity can be paired with green-emitting counterparts for use in dual-color reporter assays or can be used alone for in vivo imaging. North American firefly Photinus pyralis luciferase, which emits yellow-green light nm , has been adapted for a variety of applications, including gene reporter assays, whole-cell biosensor measurements, and in vivo imaging. Beginning with a previously reported red-emitting thermostable mutant and using mutagenesis techniques, we engineered two luciferases with redder emission maxima while maintaining satisfactory specific activities and thermostability. Light emission from the North American firefly Photinus pyralis, which emits yellow-green nm light, is widely believed to be the most efficient bioluminescence system known, making this luciferase an excellent tool for monitoring gene expression.
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