ChemInform Abstract: P-NITROBENZOIC ACID BY NITRATION AND OXIDATION OF PHENYLALKANES

1978 ◽  
Vol 9 (14) ◽  
Author(s):  
C. S. JUN. RONDESTVEDT ◽  
J. R. JEFFREY ◽  
J. E. MILLER
Keyword(s):  
Nitrobenzoic Acid

Synthesis and Herbicidal Activities of Novel Thiazole PPO Inhibitors

2020 ◽  
Vol 17 (2) ◽  
pp. 192-198
Author(s):  
Shu Chen ◽  
Guihua Ren ◽  
Dan Pei ◽  
Fan Zhang ◽  
Jie Liu ◽  
...  
Keyword(s):  
Petri Dish ◽  
Amaranthus Retroflexus ◽  
Inhibition Rate ◽  
Culture Dish ◽  
Protoporphyrinogen Oxidase ◽  
Nitrobenzoic Acid ◽  
Different Types ◽  
Key Enzyme ◽  
Stem Leaf ◽  
Spray Treatment

Background: Protoporphyrinogen oxidase (PPO, EC 1.3.3.4) is a key enzyme in the biosynthesis of chlorophyll and heme, also the target of different types of herbicides. Thiazole compounds shown excellent biological activity, can be designed by using active groups docking for new PPO inhibitors. Objective: The objective of this study was to synthsize a series of aryl thiazole compounds as PPO inhibitors. Methods: In this study, a series of aryl thiazole compounds derivatives 11a-l were obtained from 2- chloro-5-nitrobenzoic acid as the starting material via esterification, Iron powder reduction, diazotization, Hantzsch reaction and final acylation. All synthesized compounds have been tested for their herbicidal activities as a PPO inhibitors. Results: The Petri dish test indicated that all compounds exhibited good herbicidal activities at 200 mg/L using culture dish. And the post-emergence tests showed that at 150g.ai/ha on weed stem leaf spray treatment, some of the title compounds exhibited 80% inhibition rate against the dicotyledonou weeds Amaranthus retroflexus and Eclipta prostrate. Conclusion: Good activity was noted for some compounds that compounds 11a, 11b, 11c, 11g, 11h had 80% inhibition on stems and leaves of Amaranthus retroflexus at 150g.ai/ha.

The effect of polymeric and model imidazolium halides on the rate of hydrolysis of 4-acetoxy-3-nitrobenzoic acid

1985 ◽  
Vol 50 (4) ◽  
pp. 845-853 ◽  
Author(s):  
Miloslav Šorm ◽  
Miloslav Procházka ◽  
Jaroslav Kálal
Keyword(s):  
Catalyst Concentration ◽  
Low Molecular Weight ◽  
Imidazolium Chloride ◽  
First Order ◽  
Nitrobenzoic Acid ◽  
Rate Of Hydrolysis ◽  
Acid Catalyzed ◽  
Hydrolysis Of ◽  
Ethanol In Water ◽  
Direct Attack

The course of hydrolysis of an ester, 4-acetoxy-3-nitrobenzoic acid catalyzed with poly(1-methyl-3-allylimidazolium bromide) (IIa), poly[l-methyl-3-(2-propinyl)imidazolium chloride] (IIb) and poly[l-methyl-3-(2-methacryloyloxyethyl)imidazolium bromide] (IIc) in a 28.5% aqueous ethanol was investigated as a function of pH and compared with low-molecular weight models, viz., l-methyl-3-alkylimidazolium bromides (the alkyl group being methyl, propyl, and hexyl, resp). Polymers IIb, IIc possessed a higher activity at pH above 9, while the models were more active at a lower pH with a maximum at pH 7.67. The catalytic activity at the higher pH is attributed to an attack by the OH- group, while at the lower pH it is assigned to a direct attack of water on the substrate. The rate of hydrolysis of 4-acetoxy-3-nitrobenzoic acid is proportional to the catalyst concentration [IIc] and proceeds as a first-order reaction. The hydrolysis depends on the composition of the solvent and was highest at 28.5% (vol.) of ethanol in water. The hydrolysis of a neutral ester, 4-nitrophenyl acetate, was not accelerated by IIc.

THE IONIZATION CONSTANTS OF p-NITROPHENYLACETIC AND PHENYLMALONIC ACIDS

1933 ◽  
Vol 8 (5) ◽  
pp. 447-449 ◽  
Author(s):  
Steward Basterfield ◽  
James W. Tomecko
Keyword(s):  
Benzoic Acid ◽  
Nitro Group ◽  
Malonic Acid ◽  
Phenylacetic Acid ◽  
Ionization Constants ◽  
Side Chain ◽  
Cooh Group ◽  
Conductivity Data ◽  
Nitrobenzoic Acid ◽  
Phenylmalonic Acid

The ionization constants of p-nitrophenylacetic and phenylmalonic acids have been determined from conductivity data. The value of K for p-nitrophenylacetic acid at 25 °C. is 1.04 × 10−4, about twice that of phenylacetic acid. The nitro group in the nucleus has not as powerful an effect on the ionization when the COOH group is in the side chain as it has when both nitro group and COOH are in the nucleus. K for p-nitrobenzoic acid is six times as great as K for benzoic acid. K for phenylmalonic acid is 2. 77 × 10−3 as compared with 1.6 × 10−3 for malonic acid.

Crystal structure of 3,5-dimethyl-4-nitrobenzoic acid

1973 ◽  
Vol 29 (12) ◽  
pp. 2658-2664 ◽  
Author(s):  
M. C. Apreda ◽  
P. Smith-Verdier ◽  
S. García-Blanco
Keyword(s):  
Crystal Structure ◽  
Nitrobenzoic Acid

The Interactions of adenylates with allosteric citrate synthase

1979 ◽  
Vol 57 (5) ◽  
pp. 385-395 ◽  
Author(s):  
Michael M. Talgoy ◽  
Harry W. Duckworth
Keyword(s):  
Coenzyme A ◽  
Citrate Synthase ◽  
Potent Inhibitor ◽  
Sulfhydryl Group ◽  
Fluorescence Technique ◽  
Allosteric Site ◽  
Acetyl Coenzyme A ◽  
Nitrobenzoic Acid ◽  
Adenylic Acid ◽  
Derivatives Of

Evidence is presented that a number of derivatives of adenylic acid may bind to the allosteric NADH binding site of Escherichia coli citrate synthase. This evidence includes the facts that all the adenylates inhibit NADH binding in a competitive manner and that those which have been tested protect an enzyme sulfhydryl group from reaction with 5,5′-dithiobis-(2-nitrobenzoic acid) in the same way that NADH does. However, whereas NADH is a potent inhibitor of citrate synthase, most of the adenylates are activators. The best activator, ADP-ribose, increases the affinity of the enzyme for the substrate, acetyl-CoA, and saturates the enzyme in a sigmoid manner. A fluorescence technique, involving the displacement of 8-anilino-1-naphthalenesulfonate from its complex with citrate synthase, is used to obtain saturation curves for several nucleotides under nonassay conditions. It is found that acetyl-coenzyme A, coenzyme A, and ADP-ribose all bind to the enzyme cooperatively, and that the binding of each becomes tighter in the presence of KCl the activator, and oxaloacetic acid (OAA), the second substrate. Another inhibitor, α-ketoglutarate, can compete with OAA in the absence of KClbut not in its presence. The nature of the allosteric site of citrate synthase, and the modes of action of several activators and inhibitors, are discussed in the light of this evidence.

scholarly journals Identification of 5,5'-dithio-bis-2-nitrobenzoic acid (DTNB) and alkali light chains of piscine myosin.

1982 ◽  
Vol 48 (6) ◽  
pp. 827-832 ◽  
Author(s):  
Shugo WATABE ◽  
Yoshihior OCHIAI ◽  
Kanehisa HASHIMOTO
Keyword(s):  
Light Chains ◽  
Nitrobenzoic Acid
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