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. Author manuscript; available in PMC: 2021 Mar 1.
Published in final edited form as: Sens Actuators B Chem. 2019 Nov 30;306:127446. doi: 10.1016/j.snb.2019.127446

Figure 4. Evaluation of the Photophysical, Spectroscopic, and Selectivity Properties of NO2-Rosol.

Figure 4.

A) Fluorescence activation of NO2-Rosol (20 μM) with and without NTR (10 μg/mL) and/or NADPH (500 μM) in 95:5 PBS:DMSO (λex = 550 nm); B) Fluorescence intensity of NO2-Rosol (20 μM) with and without NTR that had been pre-treated with various concentrations of a standard NTR inhibitor (dicoumarol) in the presence of NADPH (500 μM); C) Measurement of the fluorescence intensity of NO2-Rosol upon its activation using various concentrations of NTR (0–10 μg/mL) and a constant concentration of NADPH (500 μM); D) Normalized absorption spectrum of NADPH separately (black) and with NO2-Rosol both before (blue) and 60 min after (red) the addition of NTR (10 μg/mL); E) Fluorescence intensity of NO2-Rosol in the presence of NTR (10 μg/mL) and other biologically-relevant small molecules, all of which are in the presence of NADPH (500 μM): H2O2, NaOCl (100 μM each); Cys, HCys, GSH, Glut, Lys, ascorbic acid, Gly (1 mM each); MgCl2 (2 mM); KOAc, NaOAc (50 mM each); F) Competition assay involving NO2-Rosol with and without NTR and/or other biologically-relevant enzymes (10 μg/mL), wherein each arrangement includes the presence of NADPH (500 μM). Lys = lysine, Gly = glycine, Glut = glutamate, GSH = glutathione (reduced form), HCys = homocysteine, Cys = Cysteine, G = glutathione reductase, L = leucine dehydrogenase, C = Cytochrome c reductase. Practical considerations required the use of a Type I NTR in performing all solution studies.