Preparation of optically active aromatic sulphoxides of high optical purity by the direct oxidation of the sulphides in the presence of bovine serum albumin

Sugimoto, Toyonari; Kokubo, Toshio; Miyazaki, Jinsei; Tanimoto, Shigeo; Okano, Masaya

doi:10.1039/c39790000402

Cited by 46 publications

(22 citation statements)

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“…Sugimoto oxidised a number of aromatic sulfides in the presence of bovine serum albumin (BSA) using sodium metaperiodate as the oxidant. 163 The results obtained were impressive with 162 being obtained with an optical purity of 81% (Scheme 66).…”

Section: Scheme 65mentioning

confidence: 56%

Synthesis of enantioenriched sulfoxides

O’Mahony¹,

Kelly²,

Lawrence³

et al. 2011

Arkivoc

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This review discusses strategies for the asymmetric synthesis of sulfoxides, compounds with many applications in stereoselective synthesis and in some cases with pharmaceutical application. The review describes asymmetric oxidation, including metal catalyzed and nonmetal and biological oxidation processes, in addition to synthetic approaches via nucleophilic substitution of appropriately substituted precursors. Kinetic resolution in oxidation of sulfoxides to the analogous sulfones is also discussed; in certain instances, access to enantioenriched sulfoxides can be achieved via a combination of asymmetric sulfide oxidation and complementary kinetic resolution in sulfoxide oxidation.

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Section: Scheme 65mentioning

confidence: 56%

Synthesis of enantioenriched sulfoxides

O’Mahony¹,

Kelly²,

Lawrence³

et al. 2011

Arkivoc

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“…In this context of supramolecular anchoring of cofactors, serum albumin plays a key role; it functions as a transport protein in plasma and shows a unique ability to bind a variety of hydrophobic molecules, including steroids, fatty acids and heme. [29] In addition, serum albumins, especially the bovine one, have been shown to catalyze enantioselective transformations such as oxidations, [30,31] reductions [32] and Diels-Alder cycloadditions with moderate to good enantioselectivity. [33] We have chosen Mn-salen catalysts, which are well-known systems for selective oxidation catalysis in organic solvents, because of their broad catalytic properties.…”

Section: Resultsmentioning

confidence: 99%

The Protein Environment Drives Selectivity for Sulfide Oxidation by an Artificial Metalloenzyme

et al. 2009

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MAGIC Mn-salen mETALLOZYME: The design of an original, artificial, inorganic, complex-protein adduct, has led to a better understanding of the synergistic effects of both partners. The exclusive formation of sulfoxides by the hybrid biocatalyst, as opposed to sulfone in the case of the free inorganic complex, highlights the modulating role of the inorganic-complex-binding site in the protein. Artificial metalloenzymes based on the incorporation of Mn-salen complexes into human serum albumin display high efficiency and selectivity for sulfoxide production during sulfide oxidation. The reactions carried out by the artificial metallozymes are comparable to those carried out by natural biocatalysis. We have found that the polarity of the protein environment is crucial for selectivity and that a synergy between both partners of the hybrid results in the novel activity.

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“…Helminthosporiurn species failed to oxidize the aryl benzyl sulfides 8 and 9, the low isolated yields of racemic sulfoxide being possibly the result of autooxidation, but gave consistently the (S) enantiomer of alkyl benzyl sulfoxides, with the exception of benzyl isopropyl sulfoxide (13), which was formed as the racemate. In the case of oxidation of benzyl n-propyl sulfide (12), the low yield of close to racemic material prompted us to carry out a control incubation using autoclaved fungus, but no autooxidation was apparent.…”

Section: Introductionmentioning

confidence: 99%

“…The general preference of M. isabellina for the production of (R) sulfoxides, established for the bioconversion of alkyl aryl sulfides (I), is seen in the bioconversion of benzyl isopropyl sulfide (13), where the (R) sulfoxide is obtained in an enantiomeric excess of 59%. Benzyl tert-butyl sulfide (15) is, however, oxidized to give predominantly the (S) enantiomer.…”

Section: Introductionmentioning

confidence: 99%

Microbial oxidation of benzyl sulfides and bibenzyl by Mortierella isabellina and Helminthosporium species

Holland¹,

Rand²,

Viski³

et al. 1991

Can. J. Chem.

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. Can. J. Chem. 69, 1989Chem. 69, (1991. The biotransformation of 1,2-diphenylethane by the fungus Mortierella isabellina ATCC 42613, and that of a series of alkyl benzyl sulfides by the fungi M. isabellina and Helminthosporium species NRRL 4671 have been studied. Mortierella hydroxylates 1,2-diphenylethane in low yield, giving (9-1,2-diphenylethanol with an enantiomeric purity of 33%. Bioconversions of deuterium-labelled and racemic 1,2-diphenylethanol by M. isabellina demonstrate that this organism performs reversible oxidation/reduction of the alcohol. Biotransformations of n-alkyl benzyl sulfides by H. species give predominantly the (S) enantiomer of sulfoxide, with no sulfone formation, but M. isabellina, although showing a general preference for the oxidation of alkyl benzyl sulfides to (R) sulfoxides, also generates sulfones from n-alkyl benzyl sulfides in a time-dependent manner that suggests a stereoselective removal of (R) sulfoxide. The latter microorganism can be used, however, for the production of (R)-benzyl methyl and benzyl isopropyl sulfoxides, and gives (S)-benzyl tert-butyl sulfoxide in low yield.

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Preparation of optically active aromatic sulphoxides of high optical purity by the direct oxidation of the sulphides in the presence of bovine serum albumin

Cited by 46 publications

References 0 publications

Synthesis of enantioenriched sulfoxides

Synthesis of enantioenriched sulfoxides

The Protein Environment Drives Selectivity for Sulfide Oxidation by an Artificial Metalloenzyme

Microbial oxidation of benzyl sulfides and bibenzyl by Mortierella isabellina and Helminthosporium species

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