830-03-5

Basic information

• Product Name: 4-NITROPHENYL ACETATE
• Synonyms: 4-Nitrophenylacetat;4-Nitropheyl acetate;Acetic acid, p-nitrophenyl ester;aceticacid,p-nitrophenylester;Essigsαure-4-nitrophenylester;Phenol, p-nitro-, acetate;Phenol,p-nitro-,acetate;p-Nitrobenzene acetate
• CAS NO: 830-03-5
• Molecular Formula: C₈H₇NO₄
• Molecular Weight: 181.15
• EINECS: 212-593-5
• Product Categories: NA - NI;Alphabetic;Analytical Standards;Analytical/Chromatography;Bioactive Small Molecules;Building Blocks;C8 to C9;Carbonyl Compounds;Cell Biology;Chemical Synthesis;Esters;N;Organic Building Blocks
• Mol File: 830-03-5.mol
• Article Data: 166

Chemical Properties

• Melting Point: 75-77 °C(lit.)
• Boiling Point: 314.24°C (rough estimate)
• Flash Point: 145.2°C
• Appearance: Green/Powder
• Density: 1.4283 (rough estimate)
• Vapor Pressure: 0.0014mmHg at 25°C
• Refractive Index: 1.5468 (estimate)
• Storage Temp.: −20°C
• Solubility: 0.53g/l
• Water Solubility: Insoluble in water.
• Stability: Stable. Combustible. Incompatible with strong oxidizing agents.
• BRN: 515874
• CAS DataBase Reference: 4-NITROPHENYL ACETATE(CAS DataBase Reference)
• NIST Chemistry Reference: 4-NITROPHENYL ACETATE(830-03-5)
• EPA Substance Registry System: 4-NITROPHENYL ACETATE(830-03-5)

Safety Data

• Hazard Codes: F,C
• Statements: 11-34
• Safety Statements: 24/25-45-36/37/39-26-16
• WGK Germany: 3
• RTECS: AJ1150000
• TSCA: Yes
• Hazardous Substances Data: 830-03-5(Hazardous Substances Data)

Usage

Uses

Used in Enzyme Activity Assays:
4-Nitrophenyl Acetate is used as a substrate to study the enzymatic activity of Carbonic Anhydrase III isolated from bovine skeletal muscle. The release of the 4-nitrophenolate ion upon hydrolysis allows for the quantification of enzyme activity and provides insights into the enzyme's catalytic properties.
Used in Peptide Chemistry:
In the field of peptide chemistry, 4-Nitrophenyl Acetate is used with iodoacetic acid for the reductive cleavage of methionine-containing peptides. This application aids in the analysis and manipulation of peptide sequences, facilitating the study of protein structure and function.
Used in Esterase and Lipase Assays:
4-Nitrophenyl Acetate serves as a substrate in assays for esterase and lipase activity. The yellow-colored product formed upon hydrolysis allows for the easy detection and quantification of enzyme activity, making it a valuable tool in the study of these enzymes and their potential applications.
Used in Inorganic Complex Evaluation:
In the study of inorganic complexes, 4-Nitrophenyl Acetate is utilized to evaluate the methanolysis or hydrolysis activity of these complexes. The release of the 4-nitrophenolate ion provides a means to assess the catalytic efficiency and selectivity of the inorganic complexes in ester hydrolysis reactions.

Synthesis Reference(s)

Synthesis, p. 991, 1981 DOI: 10.1055/s-1981-29674

Purification Methods

Recrystallise the ester from absolute EtOH [Moss et al. J Am Chem Soc 108 5520 1986]. [Beilstein 6 IV 1298.]

InChI:InChI=1/C8H7NO4/c1-6(10)13-8-4-2-7(3-5-8)9(11)12/h2-5H,1H3

Upstream product

• 463-51-4 Ketene 
• 100-02-7 4-nitro-phenol 
• 108-24-7 acetic anhydride 
• 878-00-2 4-formylphenyl acetate 
• 14609-74-6 p-nitrophenolate 
• 37441-95-5 1-(2-thioxobenzo[d]oxazol-3(2H)-yl)ethanone 
• 64-19-7 acetic acid 
• 75-15-0 carbon disulfide 
• 7446-70-0 aluminium trichloride 
• 100-17-4 para-methoxynitrobenzene 
• 75-36-5 acetyl chloride 
• 108-22-5 Isopropenyl acetate 
• 108-05-4 vinyl acetate 
• 777-84-4 chloroacetic acid 4-nitrophenyl ester 

Downstream Products

• 13871-68-6 p-aminophenyl acetate 
• 1450-76-6 1-(2-hydroxy-5-nitrophenyl)ethanone 
• 79030-44-7 4,4'-diacetoxyazoxybenzene 
• 64330-82-1 2-Acetoxypropyl-p-nitrophenylether 
• 39570-13-3 N^α-Acetyl-N^β-o-hydroxybenzalhydrazinoessigsaeure-ethylester 
• 62486-17-3 Acetic acid 2-cyano-1,2-dimethyl-2-phenyl-ethyl ester 
• 14906-56-0 4-Acetamino-pyridin-1-oxid 
• 100-02-7 4-nitro-phenol 
• 30355-53-4 N-(amino-methyl-[1,3,5]triazin-2-yl)-acetamide 
• 6304-89-8 3-acetoxybenzoic acid 
• 14609-74-6 p-nitrophenolate 
• 74069-32-2 C₄₂H₇₀O₃₅*C₈H₇NO₄ 
• 4201-66-5 methyl 6-O-acetyl-α-D-glucopyranoside 
• 1218-34-4 N-AcTrp 

Relevant articles and documents

Simple Design of an Enzyme-Inspired Supported Catalyst Based on a Catalytic Triad

Enzyme active sites afford an intricate interplay of functional groups to mediate complex organic and inorganic reactions. Many hydrolytic enzymes use a catalytic triad comprising three different functional residues—(Ser(-OH), Hist(-imidazole), Asp(-CO2H))—that catalyze the hydrolysis of numerous unique substrates. Inspired by this design, we have developed a simple one-step synthesis for preparing a new supported catalytic system in which the three reactive groups of the catalytic triad (alcohol, imidazole, and carboxylate) are incorporated into a single functional unit. These artificial active sites can be coupled to a solid-phase support (Merrifield resin) by copper(I)-catalyzed azide-alkyne cycloaddition “click chemistry,” and their effectiveness as esterolysis catalysts was demonstrated. Furthermore, tuning the local hydrophobicity of the resin particles with an approach analogous to the native enzyme hydrophobic pocket increased the catalytic efficiency. Quantum mechanics and molecular dynamics computational modeling were used to probe the catalytic effect and suggested a concerted two-step mechanism and hydrophobic nanoenvironment similar to that of hydrolytic enzymes.

Protonic Reorganization in Catalysis by Serine Proteases: Acylation by Small Substrates

The pH (pD)-rate profiles for acylation of α-lytic protease in protium and deuterium oxides by p-nitrophenyl acetate show pK values of 5.92 and 6.60, well below the enzyme ionization pK values of 6.70 and 7.35.This is attributed to a pH-induced change in the rate-determining step.The data are consistent with an initial acylation of active-site histidine (protolytically assisted, kH/kD = 2.4), followed by an intramolecular N -> O acyl shift to active-site serine by parallel specific-acid-catalyzed (kH/kD = 0.5) and general-acid-catalyzed (kH/kD = 2) routes.The magnitude of pK(D2O) - pK(H2O) and a proton inventory of the general-acid-catalyzed N -> O acyl shift both suggest that deprotonation of α-lytic protease generates an unusual protonic site with a "loosely bound" proton.The β-deuterium isotope effect, k3H/k3D = 0.98, for the same step confirms nucleophilic interaction at carbonyl in the transition state.An abbreviated proton inventory for acylation of α-chymotrypsin by p-nitrophenyl acetate is consistent with a "loosely bound" proton there also.A proton inventory for acylation of elastase by N-(carbobenzyloxy)-L-alanine p-nitrophenyl ester is linear, suggesting one-proton catalysis and indicating that if "loosely bound" reactant-state protons are present, they are catalytically silent.The general picture, from this work and that of others, is that the catalytic response of serine proteases to small, "unnatural" substrates is highly variable, both in site of nucleophilic attack and involvement of protolytic catalysis.Probably mutual transition-state interactions over an extended region of both enzyme and natural-substrate structure are required to bring into active function the full catalytic capability with which the serine proteases have been endowed by biological evolution.

Palladium-catalyzed aryl group transfer from triarylphosphines to arylboronic acids

A study of Pd-catalyzed arylation of arylboronic acids with triarylphosphines is presented. Various parameters of this transformation, such as the oxygen presence, choice of solvent, temperature, palladium source, bases and oxidants, were tested and the optimal conditions of the aryl transfer were determined. The effect of electron-withdrawing and electron-donating substituents on the aryl groups of both reactants was also investigated. The unusual transfer of the acetate group from Pd(OAc)2 to p-nitrophenylboronic acid in the presence of PAr3 is reported. A plausible mechanism of the Pd-catalyzed aryl group transfer from PAr3 to the arylboronic acid is proposed.

Efficient Assay for the Detection of Hydrogen Peroxide by Estimating Enzyme Promiscuous Activity in the Perhydrolysis Reaction

Hydrogen peroxide is an ideal oxidant in view of its availability, atom economy, or green aspects. Furthermore, it is produced by the cell mitochondria and plays a meaningful role in controlling physiological processes, but its unregulated production leads to the destruction of organs. Due to its diverse roles, a fast and selective method for hydrogen peroxide detection is the major limitation to preventing the negative effects caused by its excess. Therefore, we aimed to develop an efficient assay for the detection of H2O2. For this purpose, we combined the enzymatic method for the detection of hydrogen peroxide with the estimation of the promiscuity of various enzymes. We estimated the activity of an enzyme in the reaction of p-nitrophenyl esters with hydrogen peroxide resulting in the formation of peracid. To our knowledge, there is no example of a simple, multi-sensor demonstrating the promiscuous activity of an enzyme and detecting hydrogen peroxide in aqueous media.

Prodrug compound and application ofprodrug compound in treatment of cancer

The present invention provides a compound indicated by a formula (I), pharmaceutically acceptable salts or esters thereof, a pharmaceutical composition of the compound, and application of the compoundand the pharmaceutical composition in the inhibition or regulation of the activity of tyrosine kinase and treating disease symptoms or symptoms including cancer mediated by tyrosine kinase.

PRODRUGS OF THE TYROSINE KINASE INHIBITOR FOR TREATING CANCER

There are provided compounds of Formula (I), and pharmaceutically acceptable salts and esters thereof, and pharmaceutical compositions thereof, useful for inhibition or modulation of the activity of tyrosine kinases and treatment of disease states or conditions mediated by tyrosine kinases, including cancers. (I)

Tropolonate salts as acyl-transfer catalysts under thermal and photochemical conditions: Reaction scope and mechanistic insights

Acyl-transfer catalysis is a frequently used tool to promote the formation of carboxylic acid derivatives, which are important synthetic precursors and target compounds in organic synthesis. However, there have been only a few structural motifs known to efficiently catalyze the acyl-transfer reaction. Herein, we introduce a different acyl-transfer catalytic paradigm based on the tropolone framework. We show that tropolonate salts, due to their strong nucleophilicity and photochemical activity, can promote the coupling reaction between alcohols and carboxylic acid anhydrides or chlorides to give products under thermal or blue light photochemical conditions. Kinetic studies and density functional theory calculations suggest interesting mechanistic insights for reactions promoted by this acyl-transfer catalytic system.

Organocatalytic Control over a Fuel-Driven Transient-Esterification Network**

Signal transduction in living systems is the conversion of information into a chemical change, and is the principal process by which cells communicate. In nature, these functions are encoded in non-equilibrium (bio)chemical reaction networks (CRNs) controlled by enzymes. However, man-made catalytically controlled networks are rare. We incorporated catalysis into an artificial fuel-driven out-of-equilibrium CRN, where the forward (ester formation) and backward (ester hydrolysis) reactions are controlled by varying the ratio of two organocatalysts: pyridine and imidazole. This catalytic regulation enables full control over ester yield and lifetime. This fuel-driven strategy was expanded to a responsive polymer system, where transient polymer conformation and aggregation are controlled through fuel and catalyst levels. Altogether, we show that organocatalysis can be used to control a man-made fuel-driven system and induce a change in a macromolecular superstructure, as in natural non-equilibrium systems.

Preparation method for phenyl acetate compound

The invention discloses a preparation method for a phenyl acetate compound. The preparation method comprises the following steps: taking substituted phenol shown as formula (I) and acetic anhydride asreaction raw materials, taking a sodium hydroxide aqueous solution as a solvent, and performing esterification reaction in a tubular reactor, thereby acquiring the phenyl acetate compound shown as formula (II). The reaction formula is as follows. In formula (I) and formula (II), substituent group R is hydrogen, C1-C6 alkyl, nitro, cyano group, halogen, carboxyl or C1-C12 alkoxycarbonyl. The manner of approximate plug flow tubular reaction is adopted by the invention, so that materials in tubular reaction almost are free from back mixing, mass and heat transfer efficiency is high, happening ofside reaction is obviously reduced and product yield and purity are both higher.

Manganese-mediated acetylation of alcohols, phenols, thiols, and amines utilizing acetic anhydride

Manganese(II) chloride-catalyzed acetylation of alcohols, phenols thiols and amines with acetic anhydride is reported. This method is environment-friendly and economically viable as it involves inexpensive, relatively benign catalyst, mild reaction condition, and simple workup. Acetylation is performed under the solvent-free condition at ambient temperature and acetylated products obtained in good to excellent yields. Primary, secondary heterocyclic amines, and phenols with various functional groups are smoothly acetylated in good yields. This method exhibits exquisite chemoselectivity, the amino group is preferentially acetylated in the presence of a hydroxyl/thiol group.