148519-91-9

Basic information

• Product Name: [1,1-Biphenyl]-2,3-diol, 2-amino- (9CI)
• Synonyms: [1,1-Biphenyl]-2,3-diol, 2-amino- (9CI)
• CAS NO: 148519-91-9
• Molecular Formula: C₁₂H₁₁NO₂
• Molecular Weight: 202.22918
• Product Categories: ALCOHOL
• Mol File: 148519-91-9.mol
• Article Data: 1

Chemical Properties

• Appearance: /
• CAS DataBase Reference: [1,1-Biphenyl]-2,3-diol, 2-amino- (9CI)(CAS DataBase Reference)
• NIST Chemistry Reference: [1,1-Biphenyl]-2,3-diol, 2-amino- (9CI)(148519-91-9)
• EPA Substance Registry System: [1,1-Biphenyl]-2,3-diol, 2-amino- (9CI)(148519-91-9)

Safety Data

• Hazardous Substances Data: 148519-91-9(Hazardous Substances Data)

Usage

General Description

[1,1-Biphenyl]-2,3-diol, 2-amino- (9CI) is a chemical compound with the molecular formula C12H11NO2. It is a derivative of 1,1-Biphenyl with an amino group attached to the 2-position of the phenyl ring. [1,1-Biphenyl]-2,3-diol, 2-amino- (9CI) has potential applications in the pharmaceutical and chemical industries, where it can be used as a building block for the synthesis of various organic compounds. Its unique structure and reactivity make it a valuable intermediate for the production of dyes, pharmaceuticals, and other fine chemicals. Studies have also shown that this compound exhibits potential biological activities, making it a subject of interest for further research and development.

Upstream product

• 86-74-8 9H-carbazole 

Relevant articles and documents

Alteration of the substrate specificity of the angular dioxygenase carbazole 1,9a-dioxygenase

Carbazole 1,9a-dioxygenase (CARDO) consists of terminal oxygenase (CARDO-O) and electron transport components. CARDO can catalyze specific oxygenation for various substrates: angular dioxygenation for carbazole and dibenzo-p-dioxin, lateral dioxygenation for anthracene, and monooxygenation for methylene carbon of fluorene and sulfide sulfur of dibenzothiophene. To elucidate the molecular mechanism determining its unique substrate specificity, 17 CARDO-O site-directed mutants at amino acid residues I262, F275, Q282, and F329, which form the substrate-interacting wall around the iron active site by CARDO-O crystal structure, were generated and characterized. F329 replacement dramatically reduced oxygenation activity. However, several mutants produced different products from the wild-type enzyme to a large extent: I262V and Q282Y (1-hydroxycarbazole), F275W (4-hydroxyfluorene), F275A (unidentified cis-dihydrodiol of fluoranthene), and I262A and I262W (monohydroxydibenzothiophenes). These results suggest the possibility that the respective substrates bind to the active sites of CARDO-O mutants in a different orientation from that of the wild-type enzyme.