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Laurdan's microenvironmental sensitivity permits better temperature resolution (0.1‐1°C) at the expense of a more limited dynamic range that is determined solely by bilayer properties. The temperature sensitivity of NBD is based on rapid intramolecular rotations and vibrations, while laurdan relies on a slower, multistep mechanism involving bilayer rearrangement, water penetration and intermolecular processes. 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Chem., 260, 1146, 10.1016\u002FS0021-9258(20)71220-2",{"doi":831},"10.1016\u002FS0021-9258(20)71220-2",{"id":24,"text":833,"url":24,"identifiers":834},"10.1016\u002FS0091-679X(08)60188-0",{"doi":833},{"id":24,"text":836,"url":24,"identifiers":837},"10.1083\u002Fjcb.91.3.872",{"doi":836},{"id":24,"text":839,"url":24,"identifiers":840},"Pagano R. E., 1983, Intracellular translocation and metabolism of a fluorescent phosphatide acid analogue in cultured fibroblasts, J. Biol. Chem., 258, 2034, 10.1016\u002FS0021-9258(18)33093-X",{"doi":841},"10.1016\u002FS0021-9258(18)33093-X",{"id":24,"text":843,"url":24,"identifiers":844},"10.1083\u002Fjcb.99.2.742",{"doi":843},{"id":24,"text":846,"url":24,"identifiers":847},"10.1083\u002Fjcb.100.1.27",{"doi":846},{"id":24,"text":849,"url":24,"identifiers":850},"10.1083\u002Fjcb.105.4.1623",{"doi":849},{"id":24,"text":852,"url":24,"identifiers":853},"Kobayashi T., 1989, Lipid transport during mitosis. Alternate pathways for delivery of newly synthesized lipids to the cell surface, J. Biol. Chem., 264, 5966",{},{"id":24,"text":855,"url":24,"identifiers":856},"10.1016\u002F0005-2736(86)90517-1",{"doi":855},{"id":24,"text":858,"url":24,"identifiers":859},"10.1016\u002F0005-2736(88)90118-6",{"doi":858},{"id":24,"text":861,"url":24,"identifiers":862},"10.1111\u002Fj.1751-1097.1991.tb02028.x",{"doi":861},{"id":24,"text":864,"url":24,"identifiers":865},"10.1016\u002F1010-6030(93)80008-W",{"doi":864},{"id":24,"text":867,"url":24,"identifiers":868},"10.1016\u002F1010-6030(93)85048-D",{"doi":867},{"id":24,"text":870,"url":24,"identifiers":871},"10.1021\u002Fj100062a014",{"doi":870},{"id":24,"text":873,"url":24,"identifiers":874},"Parasassi T., 1986, Time‐resolved fluorescence emission spectra of laurdan in phospholipid vesicles by multifrequency phase and modulation fluorometry, Cell. Mol. 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I., 1987, Culture of Animal Cells",{},{"id":24,"text":906,"url":24,"identifiers":907},"10.1016\u002FB978-0-12-427150-0.50077-2",{"doi":906},{"id":24,"text":909,"url":24,"identifiers":910},"Rose G. G., 1954, A separable and multipurpose tissue culture chamber, Tex. Rep. Biol. Med., 12, 1074",{},{"id":912,"createTime":913,"updateTime":914,"relativeEntities":915,"slug":916,"properties":917,"entityType":243,"verifyStatus":244,"verifyTime":929,"verifyNote":245,"syncStatus":23,"languages":930,"translateLanguages":24,"viewCount":25,"primaryUrl":931,"fullTextUrl":24,"authors":932,"publicationType":322,"publisherRelationship":971,"citationCount":1009,"citationInfo":1010,"publishDate":1013,"publishYear":1011,"citationAnalyzeStatus":23,"lastCitationAnalyze":1014,"indexDatabases":24,"openAccess":24,"references":1015,"isForceReanalyzing":505},"3e2a66d0-6df8-4b9e-8d87-7ccdb5d8c7b8","2024-12-25T22:20:55.941+00:00","2026-02-03T23:39:26.290+00:00",[],"The-N-Terminal-Amino-Acid-Sequences-of-the-Firefly-Luciferase-Are-Important-for-the-Stability-of-the-Enzyme",{"keywords":918,"gsPaper":919,"openalex":921,"abstract":923,"title":925,"doi":927},{},{"VOID":920},"[\"9047043423641310967\"]",{"VOID":922},"W4240930030",{"EN":924},"\u003Cjats:title>Abstract\u003C\u002Fjats:title>\u003Cjats:p>The structural and catalytic role of the N‐terminal amino acid sequence of \u003Cjats:italic>Photinus pyralis\u003C\u002Fjats:italic> luciferase was investigated by site‐directed mutagenesis. The firefly luciferase activity of a series of deletion and site‐directed mutants in the amino‐terminal region was investigated \u003Cjats:italic>in vitro\u003C\u002Fjats:italic> and \u003Cjats:italic>in vivo.\u003C\u002Fjats:italic> The mutant luciferases were produced either by \u003Cjats:italic>in vitro\u003C\u002Fjats:italic> transcription and translation or by expressing the cDNA encoding firefly luciferase in the yeast \u003Cjats:italic>Saccha‐romyces cerevisiae\u003C\u002Fjats:italic> as a fusion protein to the galactose DNA binding domain protein. Deleting the N‐terminal amino acid residues from 3 to 10 dramatically reduced the luciferase activity to less than 1% of the wild‐type activity. A marked decrease in the activity (to 5%) was also observed with the Lys8Glu mutant. The Glyl 0Arg and ProllAla mutants showed20–30% activity compared to the wild type. On the other hand, mutant Asn6Lys retained the wild‐type activity level. Randomizing3–11 N‐terminal amino acids also showed a marked decrease in activity (1%). The mutant luciferases with extremely low levels of enzymatic activity were thermally unstable. These mutational and stability data correlate with the crystal structure of firefly luciferase in which specific amino acids in the N‐terminal region form hydrogen bonds to the amino acids in the neighboring p‐stranded sheet. Because the N‐terminal region is not part of the active site, the present results suggest that the highly conserved N‐terminal amino acid sequences of the firefly luciferase are important for stabilizing the protein in its proper conformation for optimal enzyme activity.\u003C\u002Fjats:p>",{"EN":926},"The N‐Terminal Amino Acid Sequences of the Firefly Luciferase Are Important for the Stability of the 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Effects of pH, NAD\u003Cjats:sup>+\u003C\u002Fjats:sup> and Rh(bipy)\u003Cjats:sup>3+\u003C\u002Fjats:sup>\u003Cjats:sub>3\u003C\u002Fjats:sub> concentration on the efficiency of this photoconversion process are investigated. The reaction proceeds already in aqueous solution in the absence of external electron donors but it is enhanced significantly in the presence of 10% methanol.\u003C\u002Fjats:p>",{"EN":1087},"PHOTOREDUCTION OF NAD TO NADH IN SEMICONDUCTOR 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A single transient species is observed in absorption following the flash irradiation of dilute deoxygenated aqueous alcoholic solutions of rhodamine B in hte pH range 5.5–7.0 The second‐order decay constant for this semiquinone radical is an approximate linear function of the prevailing hydrogen ion concentration, the transient persisting for a period of from several seconds in neutral solution to several hours at pH = 12.\u003C\u002Fjats:p>\u003Cjats:p>The slow rate of decay and its pH‐dependence are explained in terms of an electron or H‐atom transfer between the (unobserved) protonated and (observed) unprotonated semiquinone radical with simultaneous regeneration of hte D\u003Cjats:sup>+>\u003C\u002Fjats:sup> and production of the leuco‐dye DH:—\u003C\u002Fjats:p>\u003Cjats:p>D·+ DH·\u003Cjats:sup>+\u003C\u002Fjats:sup>→ D\u003Cjats:sup>+\u003C\u002Fjats:sup>+ DH\u003C\u002Fjats:p>\u003Cjats:p>Insofar as the reactant concentrations are controlled by the acid dissociation constant 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