ntic compoundsH NMR (H, ppm)a)MS (m/z)b) 424 (M+)7.38 (1H, dd, J=7.eight Hz), 7.28 (2H, d, J=8.five Hz), 7.26 (1H, m, J=6.1 Hz), 7.09 (2H, dd, J=7.7 Hz), six.71 (1H, dd, J=8.5 Hz), three.87 (3H, s), 2.75 (2H, t, J=6.four Hz), 2.43 (2H, s), 2.02.08 (2H, m, J=6.four Hz)M-9.73 (1H, s), 7.43 (1H, d, J=4.five Hz), 7.35 (1H, dd, J=4.five and 8.1 Hz), 7.05 (4H, dd, J=2.4 and 42.9 Hz), 6.66 (1H, d, J=8.1 Hz), 2.55.65 (2H, m), 2.60.48 (2H, m), 1.92.02 (2H, m)411 (M+H+)M-7.54 (2H, m), 7.27 (4H, dd, J=9.0 and 56.7 Hz), 6.61 (1H, d, J=8.four Hz), 3.86 (3H, s)331 (M+H+)Genuine compounds were synthesized by Kumiai Chemical Sector Co., Ltd. (Shizuoka, Japan). a) 1H NMR spectrum of fenquinotrione (in CDCl3) was measured on a JEOL JNM-LA-400 (400 MHz) spectrometer. 1H NMR 5-HT5 Receptor Agonist Synonyms spectra of M-1 and M-2 (in DMSO d6) were measured on JEOL JNM-LA-300 (300 MHz) spectrometer. b) EI-MS spectrum of fenquinotrione was measured on a JEOL JMS-SX-102. ESI-MS spectra fo M-1 and M-2 were measured on Thermo Fisher Scientific Q Exactive Focus Mass spectrometry.Vol. 46, No. 3, 24957 (2021)Mechanism of action and selectivity of fenquinotrionevested by centrifugation (six,000 g at 4 for ten min) and stored at -80 . Escherichia coli cell pellets had been suspended inside a B-PER Bacterial Protein Extraction Reagent (Thermo Fisher Scientific) containing 0.2 mg/mL lysozyme, DTT (1 mM), a protease inhibitor cocktail (Sigma-Aldrich, MO, USA), and Cryonase Coldactive Nuclease (TaKaRa Bio Inc.). This suspension was centrifuged at six,000 g at 4 for 10 min. A recombinant His-tagged AtHPPD protein was purified by affinity chromatography employing a HisTrap FF column (GE Healthcare Bioscience, NJ, USA).reaction mixture devoid of the compound was employed as a good control. Inhibition of HPPD activity was determined by comparison together with the good handle. 6. Molecular docking study The AtHPPD Adenosine A1 receptor (A1R) Agonist Storage & Stability crystal structure (PDB ID: 1TFZ) in complex with an current inhibitor, DAS8697) (2-tert-butyl-4-[3-(4methoxyphenyl)-2-methyl-4-methylsulfonylbenzoyl]-1Hpyrazol-3-one), which was obtained from the Protein Data Bank, was used because the receptor protein. Docking simulation was performed making use of the CDOCKER module of Discovery Studio ver. 4.5 (Dassault Systems, V izy-Villacoublay, France). The receptor protein was ready by eliminating the water molecules, adding hydrogen, and correcting the lacking amino acid residues employing the “Clean Protein” tool inside the “Prepare Protein” module. Later, the protein was assigned making use of a CHARMM force field. Just after removing DAS869 in the protein, its cavities have been predicted using the “From Receptor Cavities” tool in the “Define and Edit Binding Site” module. Of all of the predicted cavities, Web page 1 was chosen as the active website with reference to the position of DAS869 in 1TFZ. The obtained receptor was applied as the “Input Receptor” molecule parameter. DAS869 and fenquinotrione had been applied as the “Input Ligand” parameters. All other parameters were the default settings. 7. Phylogenetic evaluation of amino acid sequences Phylogenetic analysis on the HPPD amino acid sequences of rice, Arabidopsis, along with other plants for example corn, sorghum, wheat, barley, soybean, tomato, carrot, lettuce, rapeseed, millet, alfalfa, and velvetleaf was performed working with the ClustalW algorithm. 8. Comparison from the physicochemical properties and biological effects of fenquinotrione derivatives on plants The paddy soil was placed inside a 50 cm2 plastic pot. An acceptable amount of water was added to the soil. Monochoria vaginalis and Schoenoplectus j