81467-35-8

Basic information

• Product Name: 4-methyl-4-phenyl-1,3-oxazolidin-2-one
• CAS NO: 81467-35-8
• Molecular Formula: C₁₀H₁₁NO₂
• Molecular Weight: 177.1998
• Mol File: 81467-35-8.mol
• Article Data: 6

Chemical Properties

• Boiling Point: 387.5°C at 760 mmHg
• Flash Point: 188.1°C
• Density: 1.143g/cm³
• Vapor Pressure: 3.28E-06mmHg at 25°C
• Refractive Index: 1.531
• CAS DataBase Reference: 4-methyl-4-phenyl-1,3-oxazolidin-2-one(CAS DataBase Reference)
• NIST Chemistry Reference: 4-methyl-4-phenyl-1,3-oxazolidin-2-one(81467-35-8)
• EPA Substance Registry System: 4-methyl-4-phenyl-1,3-oxazolidin-2-one(81467-35-8)

Safety Data

• Hazardous Substances Data: 81467-35-8(Hazardous Substances Data)

Upstream product

• 51-79-6 urethane 
• 98-83-9 isopropenylbenzene 
• 1123-85-9 (RS)-2-phenyl-1-propanol 
• 22436-12-0 2-phenylpropyl azidoformate 
• 105-58-8 Diethyl carbonate 
• 81467-30-3 3-(2-Hydroxy-1-methyl-1-phenylethyl)-1,4,2-dioxazol-5-on 
• 51707-36-9 3-hydroxy-2-methyl-2-phenyl-propionic acid hydrazide 

Relevant articles and documents

Enzymatic C(sp3)-H amination: P450-catalyzed conversion of carbonazidates into oxazolidinones

Cytochrome P450 enzymes can effectively promote the activation and cyclization of carbonazidate substrates to yield oxazolidinones via an intramolecular nitrene C-H insertion reaction. Investigation of the substrate scope shows that while benzylic/allylic C-H bonds are most readily aminated by these biocatalysts, stronger, secondary C-H bonds are also accessible to functionalization. Leveraging this "non-native" reactivity and assisted by fingerprint-based predictions, improved active-site variants of the bacterial P450 CYP102A1 could be identified to mediate the aminofunctionalization of two terpene natural products with high regio- and stereoselectivity. Mechanistic studies and KIE experiments show that the C-H activation step in these reactions is rate-limiting and proceeds in a stepwise manner, namely, via hydrogen atom abstraction followed by radical recombination. This study expands the reactivity scope of P450-based catalysts in the context of nitrene transfer transformations and provides first-time insights into the mechanism of P450-catalyzed C-H amination reactions.

C?H Amination via Nitrene Transfer Catalyzed by Mononuclear Non-Heme Iron-Dependent Enzymes

Expanding the reaction scope of natural metalloenzymes can provide new opportunities for biocatalysis. Mononuclear non-heme iron-dependent enzymes represent a large class of biological catalysts involved in the biosynthesis of natural products and catabolism of xenobiotics, among other processes. Here, we report that several members of this enzyme family, including Rieske dioxygenases as well as α-ketoglutarate-dependent dioxygenases and halogenases, are able to catalyze the intramolecular C?H amination of a sulfonyl azide substrate, thereby exhibiting a promiscuous nitrene transfer reactivity. One of these enzymes, naphthalene dioxygenase (NDO), was further engineered resulting in several active site variants that function as C?H aminases. Furthermore, this enzyme could be applied to execute this non-native transformation on a gram scale in a bioreactor, thus demonstrating its potential for synthetic applications. These studies highlight the functional versatility of non-heme iron-dependent enzymes and pave the way to their further investigation and development as promising biocatalysts for non-native metal-catalyzed transformations.

Organotellurium-mediated Synthesis of Oxazolidin-2-ones from Alkenes

Phenyltellurinyl trifluoroacetate in combination with ethyl carbamate and boron trifluoride-diethyl ether reacted with alkenes in refluxed 1,2-dichloroethane, regio- and stereo-selectively giving oxazolidin-2-ones in high yields.