2207-76-3

Basic information

• Product Name: 6β-Hydroperoxycholest-4-en-3-one
• Synonyms: 6β-(Hydroperoxy)cholest-4-en-3-one;6β-Hydroperoxy-cholest-4-en-3-one;6β-Hydroperoxycholest-4-en-3-one
• CAS NO: 2207-76-3
• Molecular Formula: C₂₇H₄₄O₃
• Molecular Weight: 416.63646
• Mol File: 2207-76-3.mol

Chemical Properties

• Boiling Point: 474.91°C (rough estimate)
• Flash Point: 170.7°C
• Appearance: /
• Density: 1.0362 (rough estimate)
• Vapor Pressure: 8.95E-14mmHg at 25°C
• Refractive Index: 1.4700 (estimate)
• CAS DataBase Reference: 6β-Hydroperoxycholest-4-en-3-one(CAS DataBase Reference)
• NIST Chemistry Reference: 6β-Hydroperoxycholest-4-en-3-one(2207-76-3)
• EPA Substance Registry System: 6β-Hydroperoxycholest-4-en-3-one(2207-76-3)

Safety Data

• Hazardous Substances Data: 2207-76-3(Hazardous Substances Data)

Usage

InChI:InChI=1/C27H44O3/c1-17(2)7-6-8-18(3)21-9-10-22-20-16-25(30-29)24-15-19(28)11-13-27(24,5)23(20)12-14-26(21,22)4/h15,17-18,20-23,25,29H,6-14,16H2,1-5H3/t18-,20+,21-,22+,23+,25-,26-,27-/m1/s1

Upstream product

• 2207-76-3 6β-Hydroperoxycholest-4-en-3-one 
• 601-54-7 Δ⁵-cholesten-3-one 
• 601-54-7 Cholest-5-en-3-one 
• 57-88-5 cholesterol 

Downstream Products

• 570-89-8 6β-Hydroxycholest-4-en-3-one 
• 984-84-9 Cholest-4-ene-3,6-dione 
• 570-89-8 6α-hydroxy-cholest-4-ene-3-one 
• 2207-76-3 6α-Hydroperoxycholest-4-en-3-one 

Relevant articles and documents

Isomerization, but not oxidation, is suppressed by a single point mutation, E361Q, in the reaction catalyzed by cholesterol oxidase

The putative active site base of cholesterol oxidase from Streptomyces has been removed by site-directed mutagenesis and the mutant enzyme characterized. When glutamate-361 is mutated to a glutamine, the isomerization chemistry catalyzed by cholesterol oxidase is suppressed and the intermediate cholest-5-ene-3-one is isolated. The specific activity for oxidation is 20-fold slower than the wild-type reaction, though the specific activity for isomerization is 10000-fold slower. Furthermore, incubation of cholest-5-ene-3-one with the E361Q cholesterol oxidase resulted in the production of cholest-4-ene-6β-hydroperoxy-3-one (6%), cholest-4-ene-3,6-dione (32%), cholest-4-ene-6β-ol-3-one (36%), and cholest-4-ene-6α-hydroperoxy-3-one/cholest-4-ene-6α-ol-3-one (13%), in addition to cholest-4-ene-3-one (13%). Measurement of reaction stoichiometry eliminated the possibility that H2O2 or the C4a-hydroperoxy flavin was the oxygenation agent. It is proposed that cholest-4-ene-6-hydroperoxy-3-one is the product of radical chain autoxidation and that cholest-4-ene-3,6-dione and cholest-4-ene-6-ol-3-one are decomposition products of the hydroperoxy steroid radical. The characterization of the E361Q mutant chemistry has illuminated the importance of intermediate sequestration in enzyme catalysis. The mutant enzyme will be used to obtain information about the structure of the enzyme in the presence of the reaction intermediate. Moreover, the altered activity of E361Q cholesterol oxidase will facilitate its application in studies of cell membranes.

Allylic Hydroperoxides Formed by Singlet Oxygenation of Cholest-5-en-3-one

Cholest-5-en-3-one (I) reacts with singlet oxygen to give the hemiperketal (II) (ca. 55percent), the epimeric 6β- and 6α-hydroperoxides (III) and (IV) (ca. 30 and 8percent respectively), and the dione (V) (ca 7percent).The hemiperketal (II) does not undergo an allylic rearrangement in solution, but the hydroperoxides (III) and (IV) epimerise by a radical chain mechanism. .Stereochemical problems connected with this system have been probed by carrying out parallel experiments and molecular mechanics calculations on the corresponding derivatives of methyloctahydronaphthalenone as model compounds.