99304-37-7

Usage

Uses

Used in Pharmaceutical Industry:
5-Bromo-3-hydroxy-2-indolinone is used as an anti-cancer agent for its potential to inhibit the enzyme cyclin-dependent kinase 2 (CDK2), which plays a crucial role in cell cycle regulation. This inhibition can help in controlling the unregulated cell growth associated with cancer.
Used in Biochemical Research:
5-Bromo-3-hydroxy-2-indolinone is used as a fluorescent probe for detecting amyloid fibrils, which are implicated in neurodegenerative diseases such as Alzheimer's. Its ability to bind to these fibrils and produce a fluorescent signal can aid in the study and diagnosis of such diseases.
Used in Drug Development:
5-Bromo-3-hydroxy-2-indolinone is used as a compound of interest in drug development due to its potential therapeutic effects and diverse range of biological activities. Further research and development can lead to the creation of new drugs targeting various diseases and conditions.

InChI:InChI=1/C8H6BrNO2/c9-4-1-2-6-5(3-4)7(11)8(12)10-6/h1-3,7,11H,(H,10,12)

Upstream product

• 10075-50-0 5-bromo-1H-indole 

Downstream Products

• 99304-35-5 5-Bromo-N,O-dibutyryldioxindole 
• 99313-70-9 5-Bromo-N,O-dipropionyldioxindole 
• 99304-36-6 5-bromo-2-oxoindolin-3-yl acetate 

Relevant academic research and scientific papers

Peroxygenase and oxidase activities of dehaloperoxidase-hemoglobin from Amphitrite ornata

The marine globin dehaloperoxidase-hemoglobin (DHP) from Amphitrite ornata was found to catalyze the H2O2-dependent oxidation of monohaloindoles, a previously unknown class of substrate for DHP. Using 5-Br-indole as a representative substrate, the major monooxygenated products were found to be 5-Br-2-oxindole and 5-Br-3-oxindolenine. Isotope labeling studies confirmed that the oxygen atom incorporated was derived exclusively from H2O2, indicative of a previously unreported peroxygenase activity for DHP. Peroxygenase activity could be initiated from either the ferric or oxyferrous states with equivalent substrate conversion and product distribution. It was found that 5-Br-3-oxindole, a precursor of the product 5-Br-3-oxindolenine, readily reduced the ferric enzyme to the oxyferrous state, demonstrating an unusual product-driven reduction of the enzyme. As such, DHP returns to the globin-active oxyferrous form after peroxygenase activity ceases. Reactivity with 5-Br-3-oxindole in the absence of H2O2 also yielded 5,5′-Br2-indigo above the expected reaction stoichiometry under aerobic conditions, and O2-concentration studies demonstrated dioxygen consumption. Nonenzymatic and anaerobic controls both confirmed the requirements for DHP and molecular oxygen in the catalytic generation of 5,5′-Br2-indigo, and together suggest a newly identified oxidase activity for DHP.