75102-75-9

Usage

Uses

Used in Pharmaceutical Industry:
4-(2-amino-3-chlorophenyl)pyrrole is used as a pharmaceutical intermediate for the synthesis of various drugs and drug candidates. Its unique structure allows it to be a versatile building block in the development of new therapeutic agents.
Used in Chemical Research:
4-(2-amino-3-chlorophenyl)pyrrole is used as a research compound in the field of organic chemistry. It can be employed to study the reactivity and properties of pyrrole-based compounds, as well as to develop new synthetic methods and strategies for the preparation of complex organic molecules.
Used in Material Science:
4-(2-amino-3-chlorophenyl)pyrrole can be used as a component in the development of new materials with specific properties, such as conductive polymers, sensors, or other functional materials. Its unique structure and functional groups can contribute to the desired characteristics of these materials.
Used in Agrochemical Industry:
4-(2-amino-3-chlorophenyl)pyrrole can be used as an intermediate in the synthesis of agrochemicals, such as pesticides or herbicides. Its chemical properties can be exploited to create new compounds with improved efficacy and selectivity in controlling pests and weeds.

InChI:InChI=1/C10H9ClN2/c11-9-3-1-2-8(10(9)12)7-4-5-13-6-7/h1-6,13H,12H2

Upstream product

• 153-97-9 7-chloro-D/L-tryptophan 
• 78599-49-2 3-(2'-aminophenyl)pyrrole 
• 1126425-86-2 2-chloro-6-(1-(triisopropylsilyl)-1H-pyrrol-3-yl)aniline 
• 13420-63-8 2-chloro-6-iodobenzoic acid 
• 84483-28-3 2-chloro-6-iodoaniline 

Relevant academic research and scientific papers

Synthesis and Investigation of the Abiotic Formation of Pyonitrins A-D

Pyonitrins A-D are recently isolated natural products from the insect-associated Pseudomonas protegens strain, which were isolated from complex fractions that exhibited antifungal activity via an in vivo murine candidiasis assay. Genomic studies of Pseudomonas protegens suggested that pyonitrins A-D are formed via a spontaneous nonenzymatic reaction between biosynthetic intermediates of two well-known natural products pyochelin and pyrrolnitrin. Herein we have accomplished the first biomimetic total synthesis of pyonitrins A-D in three steps and studied the nonenzymatic formation of the pyonitrins using 15N NMR spectroscopy.

The ternary complex of PrnB (the second enzyme in the pyrrolnitrin biosynthesis pathway), tryptophan, and cyanide yields new mechanistic insights into the indolamine dioxygenase superfamily

Pyrrolnitrin (3-chloro-4-(2′-nitro-3′-chlorophenyl)pyrrole) is a broad-spectrum antifungal compound isolated from Pseudomonas pyrrocinia. Four enzymes (PrnA, PrnB, PrnC, and PrnD) are required for pyrrolnitrin biosynthesis from tryptophan. PrnB rearranges the indole ring of 7-Cl-L-tryptophan and eliminates the carboxylate group. PrnB shows robust activity in vivo, but in vitro activity for PrnB under defined conditions remains undetected. The structure of PrnB establishes that the enzyme belongs to the heme b-dependent indoleamine 2,3-dioxygenase (IDO) and tryptophan 2,3-dioxygenase (TDO) family. We report the cyanide complex of PrnB and two ternary complexes with both L-tryptophan or 7-Cl-L-tryptophan and cyanide. The latter two complexes are essentially identical and mimic the likely catalytic ternary complex that occurs during turnover. In the cyanide ternary complexes, a loop previously disordered becomes ordered, contributing to the binding of substrates. The conformations of the bound tryptophan substrates are changed from that seen previously in the binary complexes. In L-tryptophan ternary complex, the indole ring now adopts the same orientation as seen in the PrnB binary complexes with other tryptophan substrates. The amide and carboxylate group of the substrate are orientated in a new conformation. Tyr321 and Ser332 play a key role in binding these groups. The structures suggest that catalysis requires an L-configured substrate. Isothermal titration calorimetry data suggest D-tryptophan does not bind after cyanide (or oxygen) coordinates with the distal (or sixth) site of heme. This is the first ternary complex with a tryptophan substrate of a member of the tryptophan dioxygenase superfamily and has mechanistic implications.

Synthesis of pyrrolnitrin and related halogenated phenylpyrroles

A general approach to halogenated arylpyrroles, including the antifungal natural product pyrrolnitrin, is described using newly synthesized halogenated pyrroles and 2,6-disubstituted nitrobenzenes or 2,6-disubstituted anilines.

Substrate Specificity and Regioselectivity of Tryptophan 7-Halogenase from Pseudomonas fluorescens BL915

Tryptophan 7-halogenase which is involved in pyrrolnitrin biosynthesis is the first halogenating enzyme to be isolated that has substrate specificity and regioselectivity. This FADH2-dependent halogenase catalyzes the chlorination of its natural substrate tryptophan exclusively at the 7-position, a position at which direct chemical chlorination is not possible. Other substrates such as N-Ω-methyltryptamine, 5-methyltryptamine, 5-methylindole, 3-methylindole, or indole-3-acetonitrile are also chlorinated by the enzyme, whereas compounds like 1-methyltryptophan, indole-3-carboxylic acid, indole-3-acetic acid, or indole are not accepted as substrates. In addition, phenylpyrrole derivatives are also chlorinated by the enzyme. However, in contrast to tryptophan, the tryptophan and indole derivatives are chlorinated at positions 2 or/and 3 of the indole ring system and not at the 7-position. Chlorination of the phenylpyrrole derivatives also proceeds without regioselectivity and a mixture of mono- and dichlorinated products is obtained.