140630-45-1

Upstream product

• 1746-13-0 allyl phenyl ether 
• 4769-73-7 (RS)-1-chloro-3-phenyloxy-2-propanol 
• 123-20-6 vinyl n-butyrate 
• 108-05-4 vinyl acetate 
• 876-27-7 4-chlorophenyl acetate 
• 108-22-5 Isopropenyl acetate 
• 106-89-8 epichlorohydrin 
• 108-95-2 phenol 
• 940-47-6 1-chloro-3-phenoxyacetone 
• 538-43-2 3-phenoxy-1,2-propanediol 
• 51594-55-9 (R)-(-)-epichlorohydrin 
• 122-60-1 Phenyl glycidyl ether 
• 71031-03-3 (R)-phenyl glycidyl ether 
• 140428-46-2 1-chloro-3-phenoxypropan-2-yl acetate 

Downstream Products

• 71031-03-3 (2R)-1,2-epoxy-3-phenoxypropane 
• 71031-03-3 (R)-phenyl glycidyl ether 
• 4769-73-7 (RS)-1-chloro-3-phenyloxy-2-propanol 
• 82430-43-1 (S)-3-chloro-1-phenoxy-2-propanol 
• 538-43-2 3-phenoxy-1,2-propanediol 
• 112243-65-9 (S)-2-hydroxy-3-phenoxypropylamine 
• 106351-44-4 (2S)-1-Isopropylamino-3-phenoxy-2-propanol 

Relevant academic research and scientific papers

Aromatic Donor-Acceptor Interaction-Based Co(III)-salen Self-Assemblies and Their Applications in Asymmetric Ring Opening of Epoxides

Aromatic donor-acceptor interaction as the driving force to assemble cooperative catalysts is described. Pyrene/naphthalenediimide functionalized Co(III)-salen complexes self-assembled into bimetallic catalysts through aromatic donor-acceptor interactions and showed high catalytic activity and selectivity in the asymmetric ring opening of various epoxides. Control experiments, nuclear magnetic resonance (NMR) spectroscopy titrations, mass spectrometry measurement, and X-ray crystal structure analysis confirmed that the catalysts assembled based on the aromatic donor-acceptor interaction, which can be a valuable noncovalent interaction in supramolecular catalyst development.

Exploring the Biocatalytic Scope of a Novel Enantioselective Halohydrin Dehalogenase from an Alphaproteobacterium

A gene encoding halohydrin dehalogenase from an alphaproteobacterium (AbHHDH) was identified, cloned and over-expressed in Escherichia coli. AbHHDH was able to catalyze the stereoselective dehalogenation of prochiral and racemic halohydrins. It showed the highest enantioselectivity in the dehalogenation of 20?mM (R,S)-2-bromo-1-phenylethanol, which yielded (S)-2-bromo-1-phenylethanol with 99% ee and 34.5% yield. Moreover, AbHHDH catalyzed the azidolysis of epoxides with low to moderate (S)-enantioselectivity. The highest enantioselectivity (E = 18.6) was observed when (R,S)-benzyl glycidyl ether was used as the substrate. A sequential kinetic resolution catalyzed by HHDH was employed for the synthesis of chiral 1-chloro-3-phenoxy-2-propanol. We prepared enantiopure (S)-isomer with a high enantiopurity of ee > 99% and a yield of 30.7% (E-value: 21.3) by kinetic resolution of 20?mM substrate. The (S)-isomer with 99% ee readily obtained from 40 to 150?mM (R,S)-1-chloro-3-phenoxy-2-propanol. Taken together, the results of this study demonstrate the applicability of this HHDH for the production of optically active compounds. [Figure not available: see fulltext.].

Highly enantioselective CALB-catalyzed kinetic resolution of building blocks for β-blocker atenolol

Both enantiomers of 4-(3-chloro-2-hydroxypropoxy)phenyl)acetamide has been synthesized in 98.5–99% enantiomeric excess by use of lipase B from Candida antarctica as catalyst. The R-alcohol is a building block for the cardioselective β-blocker (S)-atenolol ((S)-2-(4-(2-hydroxy-3-(isopropylamino)propoxy)phenyl)acetamide. Performing kinetic resolutions of 3-chloro-1-phenoxy-2-propanol and 3-bromo-1-phenoxy-2-propanol with vinyl butanoate as acyl donor and the same CALB enzyme, but a different preparation, showed higher E-values than previously reported.

Synthesis of enantiopure epoxide by 'one pot' chemoenzymatic approach using a highly enantioselective dehydrogenase

Enantiopure α-phenethyl alcohols, including aromatic halohydrins, are important chiral building blocks. One of the best approaches to synthesise α-phenethyl alcohols is asymmetric reduction of prochiral ketones by alcohol dehydrogenases (ADHs). The obtained enantiopure halohydrin could be directly used to produce enantiopure epoxide through a base-induced ring-closure reaction, which is an attractive 'one pot' chemoenzymatic method for producing high-yield epoxide. In this study, a novel medium-chain dehydrogenase (KcDH) from Kuraishia capsulate CBS1993 was identified and characterised to show its broad substrate scope and excellent enantioselectivity. KcDH showed activities on 25 substrates of the 26 tested aromatic ketones and heteroaryl ketones, with an enantiomeric excess (ee) >99% and the highest relative activity observed with para-nitro acetophenone. Due to its high enantioselectivity for α-haloketones, a chemoenzymatic method for the synthesis of enantiopure styrene oxide (SO) and phenyl glycidyl ether (PGE) was developed through a base-induced ring-closure reaction on enantiopure halohydrin obtained with KcDH. (R)-SO and (S)-PGE were obtained in 86% and 94% analytical yield, respectively, and both epoxides were obtained with ee >99%. Thus, our results suggested that KcDH may be a promising biocatalyst for the production of multiple enantiopure α-phenethyl alcohols and epoxides.

Tuning of the electronic properties of a cyclopentadienylruthenium catalyst to match racemization of electron-rich and electron-deficient alcohols

The synthesis of a new series of cyclopentadienylruthenium catalysts with varying electronic properties and their application in racemization of secondary alcohols are described. These racemizations involve two key steps: 1) β-hydride elimination (dehydrogenation) and 2) re-addition of the hydride to the intermediate ketone. The results obtained confirm our previous theory that the electronic properties of the substrate determine which of these two steps is rate determining. For an electron-deficient alcohol the rate-determining step is the β-hydride elimination (dehydrogenation), whereas for an electron-rich alcohol the re-addition of the hydride becomes the rate-determining step. By matching the electronic properties of the catalyst with the electronic properties of the alcohol, we have now shown that a dramatic increase in racemization rate can be obtained. For example, electron-deficient alcohol 15 racemized 30 times faster with electron-deficient catalyst 6 than with the unmodified standard catalyst 4. The application of these protocols will extend the scope of cyclopentadienylruthenium catalysts in racemization and dynamic kinetic resolution. Copyright

Highly active oligomeric Co(salen) catalysts for the asymmetric synthesis of α-aryloxy or α-alkoxy alcohols via kinetic resolution of terminal epoxides

A mixture of Co(salen) macrocycles, prepared via the ring expansion metathesis oligomerization of salen-functionalized cyclooctene monomers, among the most active soluble catalysts for the hydrolytic kinetic resolution (HKR) of terminal epoxides, is exploited as the catalyst in the ring-opening of epoxides using aliphatic alcohols or phenols as nucleophiles, leading to the direct synthesis of optically active α-aryloxy alcohols or α-alkoxy alcohols. The catalyst is compared to other dimeric, oligomeric and monomeric Co(salen) complexes including a pimelate-linked macrocyclic Co(salen) catalyst and a dimeric Co(salen) catalyst referred to as a bisalen. The catalysts that contain multiple Co(salen) units within a single molecular framework allow for substantial decreases in catalyst loading compared with the monomeric catalyst. The cyclooctene-based Co(salen) macrocycle catalyst allows for good activity and enantioselectivity in the ring-opening of terminal epoxides with phenols as nucleophiles, giving enhanced turnover frequencies relative to many literature catalysts. The cyclooctene-based Co(salen) macrocycle catalyst and the bisalen catalysts are shown to be the most active in the asymmetric ring-opening of (±)1,2-epoxyhexane with methanol, out-performing the other catalysts tested. The Co(salen) macrocycle catalyst is recycled 3 times in this reaction with some loss in activity but no noteworthy change in selectivity.

Highly active new chiral Co(iii) salen catalysts immobilized by electrostatic interaction with sulfonic acid linkages on ordered mesoporous SBA-16 silica

New chiral cobalt(iii) salen complexes immobilized via HO 3S-linkers on ordered SBA-16 by electrostatic interactions showed very high activity in enantioselective ring-opening reactions of racemic epoxides.

Shifting the equilibrium of a biocatalytic cascade synthesis to enantiopure epoxides using anion exchangers

Hydroxide-loaded anion exchangers have been successfully employed to shift the equilibrium of a one-pot, two-step, two-enzyme cascade reaction affording enantiopure epoxides starting from prochiral α-chloroketones. The α-chloroketones were asymmetrically reduced employing an alcohol dehydrogenase and then transformed further to the corresponding epoxides employing halohydrin dehalogenases. Each epoxide enantiomer could be obtained with up to 93% conversion in enantiomerically pure form (>99% ee). In contrast to previous studies the amount of hydride donor (2-propanol) could be reduced due to favoured halohydrin formation in the reduction of α-chloroketones.

Highly efficient route for enantioselective preparation of chlorohydrins via dynamic kinetic resolution

(Equation Presented) Dynamic kinetic resolution (DKR) of various aromatic chlorohydrins with the use of Pseudomonas cepacia lipase (PS-C "Amano" II) and ruthenium catalyst 1 afforded chlorohydrin acetates in high yields and high enantiomeric excesses. These optically pure chlorohydrin acetates are useful synthetic intermediates and can be transformed to a range of important chiral compounds.

Stereo-complementary two-step cascades using a two-enzyme system leading to enantiopure epoxides

A novel one-pot, two-step, two-enzyme cascade is described. Pro-chiral α-chloro ketones are stereoselectively reduced to the corresponding halohydrins as an intermediate by a biocatalytic hydrogen transfer process. The intermediate is transformed to the corresponding epoxide by a non-enantioselective halohydrin dehalogenase. Thus, by combining a Prelog- or anti-Prelog alcohol dehydrogenase with a non-selective halohydrin dehalogenase, enantiopure (R)- as well as (S)-epoxides were obtained.