Regiodivergent Baeyer–Villiger Oxidation of Fused Ketones by Recombinant Whole‐Cell Biocatalysts

Mihovilovic, Marko D.; Kapitán, Peter; Kapitánová, Petra

doi:10.1002/cssc.200700069

Cited by 43 publications

(25 citation statements)

References 77 publications

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“…Different structural motifs, like aliphatic, cyclic, and polycyclic have been transformed to the corresponding esters or lactones. Despite the use of aerial oxygen under ambient reaction conditions, BVMOs display a remarkably high regio-, chemo-, and stereoselectivity (Fink et al 2011;Mihovilovic et al 2008;Snajdrova et al 2006). One remarkable example for the use of BVMOs in industry is given by Codexis, which produced Esomeprazole by applying a CHMO variant (41 mutations, 104-fold increased stability and activity) in 99 % enantioselectivity (Bong et al, 2011).…”

Section: Recent Bvmo Applications Single Enzyme Transformationsmentioning

confidence: 96%

Baeyer-Villiger oxidations: biotechnological approach

Bučko

Gemeiner

Schenkmayerová

et al. 2016

Appl Microbiol Biotechnol

101

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Baeyer-Villiger monooxygenases (BVMOs) are a very well-known and intensively studied class of flavin-dependent enzymes. Their substrate promiscuity, high chemo-, regio-, and enantioselectivity are prerequisites for the use in synthetic chemistry and should pave the way for successful industrial processes. Nonetheless, only a very limited number of industrial relevant transformations are known, mainly due to the lack of BVMOs stability and cofactor dependency. In this review, we focus on novel BVMO-mediated transformations, BVMOs in cascade type reactions, potential industrial applications, and how limitations have been tackled by the community. Special attention will be put on whole-cell immobilization strategies. We emphasize to bridge recent developments in fundamental research to industrial applications.

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Section: Recent Bvmo Applications Single Enzyme Transformationsmentioning

confidence: 96%

Baeyer-Villiger oxidations: biotechnological approach

Bučko

Gemeiner

Schenkmayerová

et al. 2016

Appl Microbiol Biotechnol

101

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“…The racemic cis -bicyclo[3.2.0]hept-2-en-6-one ( 34 ) is a well-known substrate for CHMO from Acinetobacter sp. NCIMB 9871 and for many other BVMOs (Alexander et al 2012; Alphand and Furstoss 1992; Ferroni et al 2014; Fink et al 2011; Mihovilovic et al 2005b, 2008; Rial et al 2008b). After 24 h, the BVMO Lepto oxidized this racemic substrate almost completely to equal amounts of normal and abnormal lactones (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…NCIMB 9871, the ee of each regioisomeric lactone was poor (Table 4), The oxidation of the fused ketone 35 or 36 by BVMO Lepto preferentially gave abnormal lactones. These compounds ( 35 or 36 ) have been reported as substrates on approximately 10 Type I BVMOs, and in all cases except the BVMO5 from M. tuberculosis H37Rv (Snajdrova et al 2006), approximately equal amounts of regioisomeric lactones or normal lactones have been preferentially produced (Alphand and Furstoss 1992; Fink et al 2012; Mihovilovic et al 2005a, 2008; Rial et al 2008b). …”

Section: Discussionmentioning

confidence: 99%

Cloning and characterization of the Type I Baeyer–Villiger monooxygenase from Leptospira biflexa

et al. 2017

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Baeyer–Villiger monooxygenases are recognized by their ability and high selectivity as oxidative biocatalysts for the generation of esters or lactones using ketones as starting materials. These enzymes represent valuable tools for biooxidative syntheses since they can catalyze reactions that otherwise involve strong oxidative reagents. In this work, we present a novel enzyme, the Type I Baeyer–Villiger monooxygenase from Leptospira biflexa. This protein is phylogenetically distant from other well-characterized BVMOs. In order to study this new enzyme, we cloned its gene, expressed it in Escherichia coli and characterized the substrate scope of the Baeyer–Villiger monooxygenase from L. biflexa as a whole-cell biocatalyst. For this purpose, we performed the screening of a collection of ketones with variable structures and sizes, namely acyclic ketones, aromatic ketones, cyclic ketones, and fused ketones. As a result, we observed that this biocatalyst readily oxidized linear- and branched- medium-chain ketones, alkyl levulinates and linear ketones with aromatic substituents with excellent regioselectivity. In addition, this enzyme catalyzed the oxidation of 2-substituted cycloketone derivatives but showed an unusual selection against substituents in positions 3 or 4 of the ring.Electronic supplementary materialThe online version of this article (doi:10.1186/s13568-017-0390-5) contains supplementary material, which is available to authorized users.

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“…These are regiodivergent procedures in which it is possible to obtain both regioisomeric lactones (the normal or proximal one and the abnormal or distal one) from the starting ketone. Several Baeyer-Villiger monooxygenases have been used, showing a similar clustering between cyclohexanone monooxygenase (CHMO) and [52] E. coli cells expressing cyclohexanone monooxygenase from Acinetobacter calcoaceticus NCIMB 9871 (CHMO Acineto ) are able to oxidize racemic ketone 39 into a 51:49 mixture of the normal lactone 40 and the abnormal one 41 with a global yield of 63%, both lactones being achieved with high optical purity (>95% ee). [51] Studies on this biooxidation have shown inhibitory substrate and product concentrations of 0.2-0.4 g • L -1 and 4.5-5 g • L -1 , respectively.…”

Section: Oxidation Of â-Substituted Cyclic Ketonesmentioning

confidence: 99%

3.4 Baeyer–Villiger Oxidation

de Gonzalo Calvo,

van Berkel,

Fraaije

2015

Biocatalysis in Organic Synthesis 3

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The Baeyer-Villiger oxidation, a reaction described more than 110 years ago by Alfred Baeyer and Victor Villiger, [1] is among the most well-known and commonly applied reactions in organic synthesis. [2][3][4] The reaction entails the oxidation of a carbonyl compound employing an organic peracid, finally yielding an ester or lactone. Its versatility is due to the following factors: (i) different types of carbonyl compounds, such as aldehydes and linear or cyclic ketones, can be oxidized; (ii) other functional groups are well tolerated in the substrate structure; (iii) the regiochemistry is usually predictable, with the migratory aptitude being tertiary alkyl > cyclohexyl > secondary alkyl > benzyl > phenyl > primary alkyl > methyl; (iv) the migrating group retains its configuration.The mechanism of this reaction has been widely studied. [5] In the first step of the process, the peracid performs a nucleophilic attack on the carbonyl group of the ketone, leading to a tetrahedral Criegee intermediate. After oxygen insertion and the migration of the more highly substituted group, the final product is formed. The migration of the substituent and the release of the leaving group occur in a concerted way and are usually the ratelimiting step of the reaction.The classical Baeyer-Villiger procedure using organic peracids suffers from several disadvantages. First of all, organic peracids are expensive and/or hazardous, which limits their commercial application. Peracids are powerful oxidative agents, necessitating laborious protection and deprotection steps in synthesis to prevent side reactions. Due to these issues, different methodologies for carrying out the Baeyer-Villiger oxidation have been developed using mild oxidants, such as molecular oxygen or hydrogen peroxide, in the presence of organometallic catalysts or organocatalytic compounds. [6][7][8] The recent development of biocatalysis as an alternative, useful tool in organic synthesis has allowed the application of different types of enzymes, lipases and monooxygenases, in order to perform selective Baeyer-Villiger oxidations while using mild and environmentally friendly conditions. 3.4.1 Reactions Catalyzed Indirectly by HydrolasesLipases are the most widely employed biocatalysts in organic synthesis because of their high stability, catalytic efficiency, commercial availability, and broad substrate specificity. [9] Apart from their use in hydrolytic procedures, lipases have been used in other "nonconventional" reactions, such as C-C bond formation, carbon-heteroatom bond formation, and oxidative processes. [10] Lipases have also been employed in Baeyer-Villiger oxidations, as they catalyze the perhydrolysis of carboxylic acids and esters, generating the corresponding peracids, which subsequently oxidize the target substrate. Thus, the oxidation of cyclic ketones, e.g. 1, is catalyzed by the Candida antarctica lipase B (CALB) in toluene in the presence of stoichiometric amounts of myristic acid (tetradecanoic acid) and an excess of hydrogen peroxide (Scheme 1). ...

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Regiodivergent Baeyer–Villiger Oxidation of Fused Ketones by Recombinant Whole‐Cell Biocatalysts

Cited by 43 publications

References 77 publications

Baeyer-Villiger oxidations: biotechnological approach

Baeyer-Villiger oxidations: biotechnological approach

Cloning and characterization of the Type I Baeyer–Villiger monooxygenase from Leptospira biflexa

3.4 Baeyer–Villiger Oxidation

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