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• W2519211029 endingPage "1826" @default.
• W2519211029 startingPage "1818" @default.
• W2519211029 abstract "We identified three color-shifting mutations—Phe467Ser, Glu490Val, and Glu490Lys—in the C-domain of the wild-type recombinant L. mingrelica luciferase. These mutations had moderate effect on the specific activity and thermal stability of the enzyme but changed the pH-dependence of its bioluminescence spectra. We constructed the model structures of the enzyme in three known conformations (open, adenylation, and oxidation conformation). The structural analysis and experimental data provided no evidences that these residues participate in structure-forming interactions in the open or oxidation conformation or that their mutations alter the overall structure of the enzyme. Given that the bioluminescence spectra reflect the microenvironment of the emitter (oxyluciferin in an electronically excited state), we concluded that the mutated residues affect the active site during the emission of light via short-range interactions. We found that it is only in the adenylation conformation that the residues Phe467 and Glu490 approach the N-domain, whereas the domain rotation associated with the oxidation conformation completely removes them from the active site. Therefore, the emission most likely occurs from the adenylation conformation." @default.
• W2519211029 created "2016-09-23" @default.
• W2519211029 creator A5015676984 @default.
• W2519211029 creator A5038615524 @default.
• W2519211029 date "2016-12-01" @default.
• W2519211029 modified "2023-09-27" @default.
• W2519211029 title "Color-shifting mutations in the C-domain of L. mingrelica firefly luciferase provide new information about the domain alternation mechanism" @default.
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• W2519211029 doi "https://doi.org/10.1016/j.bbapap.2016.09.007" @default.
• W2519211029 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27645709" @default.
• W2519211029 hasPublicationYear "2016" @default.
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