13252-71-6

Basic information

• Product Name: Benzoic acid, 4-(hydroxyamino)-
• Synonyms: Benzoic acid, 4-(hydroxyamino)-;4-(Hydroxyamino)benzoic acid
• CAS NO: 13252-71-6
• Molecular Formula: C₇H₇NO₃
• Molecular Weight: 153.14
• Mol File: 13252-71-6.mol
• Article Data: 12

Chemical Properties

• Melting Point: >300 °C
• Boiling Point: 365.7°Cat760mmHg
• Flash Point: 174.9°C
• Appearance: /
• Density: 1.495g/cm³
• Vapor Pressure: 5.45E-06mmHg at 25°C
• Refractive Index: 1.702
• Storage Temp.: 2-8°C
• PKA: 4.54±0.10(Predicted)
• CAS DataBase Reference: Benzoic acid, 4-(hydroxyamino)-(CAS DataBase Reference)
• NIST Chemistry Reference: Benzoic acid, 4-(hydroxyamino)-(13252-71-6)
• EPA Substance Registry System: Benzoic acid, 4-(hydroxyamino)-(13252-71-6)

Safety Data

• Hazardous Substances Data: 13252-71-6(Hazardous Substances Data)

Usage

Description

Benzoic acid, 4-(hydroxyamino)-, also known as p-hydroxyaniline or p-hydroxyaminobenzoic acid, is a derivative of benzoic acid. It is an organic compound with the molecular formula C7H7NO3. This white crystalline solid, characterized by a slightly sweet odor, is sparingly soluble in water. It is recognized for its antioxidant and UV-absorbing properties, making it a versatile intermediate in the synthesis of dyes, pharmaceuticals, and other organic compounds.

Uses

Used in Chemical Industry:
Benzoic acid, 4-(hydroxyamino)-, is used as an intermediate in the production of various dyes and organic compounds due to its reactive functional groups and ability to form a range of derivatives.
Used in Pharmaceutical Industry:
In the pharmaceutical sector, Benzoic acid, 4-(hydroxyamino)-, serves as a key intermediate for the synthesis of drugs, leveraging its chemical properties to contribute to the development of new medicinal agents.
Used in Cosmetics Industry:
Benzoic acid, 4-(hydroxyamino)-, is used as a component in hair dyes, capitalizing on its color-enhancing properties and its ability to improve the stability and performance of hair color products.
Used in Antioxidant Applications:
Due to its antioxidant properties, Benzoic acid, 4-(hydroxyamino)-, is utilized in various applications to prevent oxidative degradation, thereby extending the shelf life and maintaining the quality of products in different industries.
Used in UV-Protection Formulations:
Leveraging its UV-absorbing characteristics, Benzoic acid, 4-(hydroxyamino)-, is used in the development of sunscreens and other UV-protective products to shield the skin from harmful ultraviolet radiation.
Used in Research and Development:
In the scientific community, Benzoic acid, 4-(hydroxyamino)-, is employed in research for its potential role in the treatment and prevention of various diseases and conditions, exploring its therapeutic capabilities and interactions with biological systems.

InChI:InChI=1/C7H7NO3/c9-7(10)5-1-3-6(8-11)4-2-5/h1-4,8,11H,(H,9,10)

Upstream product

• 619-68-1 4-nitrosobenzoic acid 
• 7732-18-5 water 
• 50-81-7 ascorbic acid 
• 150-13-0 4-amino-benzoic acid 
• 6427-66-3 4-azidobenzoic acid 
• 70-18-8 GLUTATHIONE 
• 52-90-4 L-Cysteine 
• 60-29-7 diethyl ether 
• 62-23-7 4-nitro-benzoic acid 

Downstream Products

• 1017266-33-9 C₇₆H₇₆N₄O₂₀S₄ 
• 39940-81-3 N-(4-carboxyphenyl)-α-phenylnitrone 
• 619-68-1 4-nitrosobenzoic acid 
• 150-13-0 4-amino-benzoic acid 

Relevant articles and documents

Characterization of the N-oxygenase AurF from Streptomyces thioletus

AurF catalyzes the N-oxidation of p-aminobenzoic acid to p-nitrobenzoic acid in the biosynthesis of the antibiotic aureothin. Here we report the characterization of AurF under optimized conditions to explore its potential use in biocatalysis. The pH optimum of the enzyme was established to be 5.5 using phenazine methosulfate (PMS)/NADH as the enzyme mediator system, showing ～10-fold higher activity than previous reports in literature. Kinetic characterization at optimized conditions give a Km of 14.7 ± 1.1 μM, a kcat of 47.5 ± 5.4 min-1 and a kcat/Km of 3.2 ± 0.4 μM-1 min-1. PMS/NADH and the native electron transfer proteins showed significant formation of the p-hydroxylaminobenzoic acid intermediate, however H2O2 produced mostly p-nitrobenzoic acid. Alanine scanning identified the role of important active site residues. The substrate specificity of AurF was examined and rationalized based on the protein crystal structure. Kinetic studies indicate that the Km is the main determinant of AurF activity toward alternative substrates.

Unprecedented Cyclization Catalyzed by a Cytochrome P450 in Benzastatin Biosynthesis

Benzastatins have unique structures probably derived from geranylated p-aminobenzoic acids. The indoline and tetrahydroquinoline scaffolds are presumably formed by cyclization of the geranyl moiety, but the cyclization mechanism was unknown. We studied the benzastatin biosynthetic gene cluster of Streptomyces sp. RI18; functions of the six enzymes encoded by it were analyzed by gene disruption in a heterologous host and in vitro enzyme assays. We propose the biosynthetic pathway for benzastatins in which a cytochrome P450 (BezE) is responsible for the cyclization of geranylated p-acetoxyaminobenzoic acids; BezE catalyzes elimination of acetic acid to form an iron nitrenoid, nitrene transfer to form an aziridine ring, and nucleophilic addition of hydroxide ion to C-10 and chloride ion to C-9 to generate the indoline and tetrahydroquinoline scaffolds, respectively. Discovery of this enzyme, which should be termed cytochrome P450 nitrene transferase, provides an important insight into the functional diversity of cytochrome P450.

Highly selective and controllable synthesis of arylhydroxylamines by the reduction of nitroarenes with an electron-withdrawing group using a new nitroreductase BaNTR1

A new bacterial nitroreductase has been identified and used as a biocatalyst for the controllable reduction of a variety of nitroarenes with an electron-withdrawing group to the corresponding N-arylhydroxylamines under mild reaction conditions with excellent selectivity (>99%). This method therefore represents a green and efficient method for the synthesis of arylhydroxylamines.