Luciferase inhibition by a novel naphthoquinone

Bedford, Rebecca; Lepage, D.; Hoffmann, Rachel; Kennedy, Steven; Gutschenritter, Tyler; Bull, Lauren; Sujijantarat, Nanthiya; DiCesare, John C.; Sheaff, Robert J.

doi:10.1016/j.jphotobiol.2011.11.008

Cited by 16 publications

(13 citation statements)

References 35 publications

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“…In Table 2 columns 1-4, the values of K m , V max , k cat and k cat /K m , are reported. K m value of BP luciferase is in good agreement, varying of about ±3 times, with that of several other luciferases reported in literature [20][21][22], and it appears very low, indicating high affinity for the substrate. Like the most bioluminescence sea animals, BP luciferases generated blue light with a maximum emission wavelength at 475 nm (Fig.…”

Section: Bp Luciferase Apparent Kinetic Constants and Bioluminescencesupporting

confidence: 85%

Purification and characterization of a novel thermostable luciferase from Benthosema pterotum

Homaei

Mymandi

Sariri

et al. 2013

Journal of Photochemistry and Photobiology B: Biology

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a b s t r a c tA novel luciferase from Benthosema pterotum, collected from Port of Jask, close to Persian Gulf, was purified for the first time, using Q-Sepharose anion exchange chromatography. The molecular mass of the novel enzyme, measured by SDS-PAGE technique, was about 27 kDa and its K m value is 0.4 lM; both values are similar to those of other coelenterazine luciferases. B. pterotum (BP) luciferase showed maximum intensity of emitted light at 40°C, in 20 mM Tris buffer, pH 9 and 20 mM magnesium concentration. Experimental measurements indicated that BP luciferase is a relatively thermostable enzyme; furthermore it shows a high residual activity at extreme pH values. Its biological activity is strongly inhibited by 1 mM Cu 2+ , Zn 2+ and Ni 2+ , while calcium and mainly magnesium ions strongly increase BP luciferase activity. The B. pterotum luciferase generated blue light with a maximum emission wavelength at 475 nm and showed some similarity with other luciferases, while other parameters appeared quite different, in this way, confirming that a novel protein has been purified.

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Section: Bp Luciferase Apparent Kinetic Constants and Bioluminescencesupporting

confidence: 85%

Purification and characterization of a novel thermostable luciferase from Benthosema pterotum

Homaei

Mymandi

Sariri

et al. 2013

Journal of Photochemistry and Photobiology B: Biology

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“…Naphthoquinone-dependent lipid peroxidation was closely related to the enhancement of Fe 21 autooxidation [3]. Naphthoquinone has three isomers: a-(1,4), b-(1,2) and amphi- (2,6) naphthoquinone. The alkylated derivative menadione (2-methyl-1,4-naphthoquinone, MNQ, also known as vitamin K 3 ) is variously used as a coagulant, a key intermediate in the preparation of other group K vitamins, an anticancer drug, a feed additive, and a plant growth regulator [4].…”

Section: Introductionmentioning

confidence: 97%

“…In addition, aging affects a pollutant's toxicology, as the pollutant becomes increasingly sequestered in soil with time, reducing (if not eliminating) its exposure and bioavailability to living organisms. Therefore, the objectives of this study were (1) investigating the adsorption and desorption of menadione in non-aged and aged soils, (2) analyzing the effect of temperature on the adsorption and desorption of menadione in soil, and (3) uncovering possible mechanisms of menadione adsorption in soil using Fourier transform infrared (FT-IR) spectroscopy and thermodynamic calculations.…”

Section: Introductionmentioning

confidence: 99%

Effect of temperature and aging on the adsorption and desorption of menadione in soil

Gao

Gong

et al. 2017

Env Prog and Sustain Energy

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In this study, the effect of soil temperature and aging on the adsorption and desorption of menadione was investigated using the batch equilibrium method. The obtained isotherm data can be well fitted to the linearized form of the Freundlich equation, with R2 values ranging between 0.91 and 1.00. The adsorption and desorption of menadione in non‐aged (control) soil increased significantly when the temperature ranged between 15 and 37°C. Among soils that were amended with menadione and aged for 72 h, the sample with 2 μg·g−1 amendment showed significantly higher adsorption/desorption than those with 10 and 20 μg·g−1 amendments (P < 0.05). Thermodynamic and isotherm hysteresis analyses demonstrated that the sorption of menadione on the control and aged soils was a spontaneous and endothermic process. Physical sorption was the predominant mechanism, and there was negative hysteresis during desorption. Furthermore, thermodynamic calculation and infrared spectral analyses suggested that the main sorption force was hydrogen bonding in all the soil samples, and the entropy gain in the whole adsorbate‐adsorbent system was the main thermodynamic driving force. © 2017 American Institute of Chemical Engineers Environ Prog, 36: 997–1004, 2017

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“…To address this possibility, putative proteasome inhibitors were directly screened for luciferase inhibition using the Cell Titer Glo assay (Promega), in which the amount of light emitted by luciferase is directly proportional to ATP concentration. Mg132 failed to inhibit this reaction while it was completely blocked by TU100, a known luciferase inhibitor (Figure E) . Compounds 2 and 28 also decreased luciferase activity, which likely explains their inhibition in all the proteasome screens.…”

Section: Resultsmentioning

confidence: 93%

Identification of Novel Proteasome Inhibitors from an Enaminone Library

et al. 2015

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A library of structurally distinct enaminones was synthesized using sonication or Ru(II) catalysis to couple primary, secondary, and tertiary thioamides with α-halocarbonyls or α-diazocarbonyls. Screening the library for proteasome inhibition using a luciferase-based assay identified seven structurally diverse compounds. Two of these molecules targeted luciferase, while the remaining five exhibited varying potency and specificity for the trypsin-like, chymotrypsin-like, or caspase-like protease activities of the proteasome. Physiological relevance was confirmed by showing these molecules inhibited proteasomal degradation of the full-length protein substrate p21cip1 expressed in tissue culture cells. A cell viability analysis revealed that the proteasome inhibitors differentially affected cell survival. Results indicate a subset of enaminones and precursor molecules identified in this study are good candidates for further development into novel proteasome inhibitors with potential therapeutic value.

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Luciferase inhibition by a novel naphthoquinone

Cited by 16 publications

References 35 publications

Purification and characterization of a novel thermostable luciferase from Benthosema pterotum

Purification and characterization of a novel thermostable luciferase from Benthosema pterotum

Effect of temperature and aging on the adsorption and desorption of menadione in soil

Identification of Novel Proteasome Inhibitors from an Enaminone Library

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