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4-((2R,3S)-3-Oxo-3λ4-[1,3]oxathiolan-2-yl)-benzonitrile is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

121125-57-3

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121125-57-3 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 121125-57-3 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,2,1,1,2 and 5 respectively; the second part has 2 digits, 5 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 121125-57:
(8*1)+(7*2)+(6*1)+(5*1)+(4*2)+(3*5)+(2*5)+(1*7)=73
73 % 10 = 3
So 121125-57-3 is a valid CAS Registry Number.

121125-57-3Downstream Products

121125-57-3Relevant academic research and scientific papers

Enantio and diastereoselectivity of cyclohexanone monooxygenase catalyzed oxidation of 1,3-dithioacetals

Colonna, Stefano,Gaggero, Nicoletta,Carrea, Giacomo,Pasta, Piero

, p. 565 - 570 (1996)

The asymmetric oxidation of 2-substituted dithianes, dithiolanes and oxathiolanes catalyzed by cyclohexanone monooxygenase (CMO) has been examined. The introduction of substituents at the C-2 causes a decrease of the e.e. with the exception of 2-benzoyl-1,3-dithiane monosulfoxide (90% e.e). With 2-monosubstituted dithioacetals CMO yields preferentially or exclusively the trans diastereoisomer. The binding of the 1,3-dithioacetals at the active site of the enzyme is not only controlled by the sterical hindrance of the substituents in position 2 but also by the configuration at C-2. The stereoselectivity of CMO has been compared with that reported for microsomal flavin and cytochrome P-450 monooxygenases.

Oxygenation of dialkyl sulfides by a modified sharpless reagent: A model system for the flavin-containing monooxygenase

Cashman,Olsen,Bornheim

, p. 3191 - 3195 (2007/10/02)

The chemical and enzymatic S-oxygenation of 2-(p-methoxyphenyl)-1,3- dithiolane and 2-(p-cyanophenyl)-1,3-oxathiolane has been investigated. In the presence of chemical oxidizing agents (i.e., NaIO4 or H2O2), modest diaste

Chemical and Enzymatic Oxidation of 2-Aryl-1,3-oxathiolanes: Mechanism of the Hepatic Flavin-Containing Monooxygenase

Cashman, John R.,Proudfoot, John,Ho, Yen-Kuang,Chin, Marian S.,Olsen, Leslie D.

, p. 4844 - 4852 (2007/10/02)

The reaction of NaIO4, H2O2, and highly purified and microsomal hog and rat liver flavin-containing monooxygenase with 2-aryl-1,3-oxathiolanes was investigated.The ρ values determined from Hammett plots for the rate of S-oxygenation are consistent with substantial nucleophilic character for the chemical reaction but this does not preclude radical character in the reaction.For the biotransformation reactions, the data provide evidence for a minor role of cytochrome P-450 in the S-oxygenation of 2-aryl-1,3-oxathiolanes, but the flavin-containing monooxygenase represents by far the major pathway for S-oxide formation.The diastereochemical outcome of the S-oxygenation of 2-aryl-1,3-oxathiolanes was determined and, in general, hog liver flavin-containing monooxygenase demonstrated considerable S-oxygenation stereoselectivity while rat liver flavin-containing monooxygenase (FMO) was markedly less stereoselective.The presence of the minor cis S-oxide diastereomer in each case is due to incomplete diastereomeric processing by each enzyme (FMO and cytochrome P-450) and not to a competing, achiral nonenzymatic process. 2-Aryl-1,3-oxathiolane S-oxides are also oxygenated a second time by H2O2 or hog or rat liver microsomal and highly purified FMO.The immediate S,S-dioxygenated product is not stable and is rapidly converted to the corresponding benzaldehyde.That the chemical and enzymatic oxygenation of 2-aryl-1,3-oxathiolane S-oxides is much slower than its corresponding sulfide is quite apparent from the large dependence on the nature of the para substituent.The reactions of 2-aryl-1,3-oxathiolanes with H2O2 and FMO serve to demonstrate the electronic and stereochemical requirements for S-oxygenation of dialkyl sulfides and provide evidence that rat and hog liver FMO are two different forms of the same enzyme.

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