Cyclohexanone monooxygenase from 9871

Stereoselective oxygen transfer to the sulphur atom of alkyl aryl sulphides catalyzed by 2-flavoenzyme monooxygenases afforded optically active sulphoxides in high optical yields . For instance, with ethyl p-tolyl sulphide as substrate cyclohexanone monooxygenase from Actinetobacter produces predominantly (— )-(S)-sulphoxide with 64% e.e. In contrast, FAD-containing dimethylaniline monooxygenase purified from hog liver microsomes affords (+ )-(i )-enantiomer of this sulphoxide with 90% optical purity . ... 

Doig, S.D., O Sullivan, L.M., Patel, S., Ward, J.M. and Woodley, J.M., Large scale production of cyclohexanone monooxygenase from Escherichia coli TOPIO pQR239. Enzyme Microb. TechnoL, 2001, 28, 265. 

Monooxygenases have been used for the Baeyer-Villiger oxidations to obtain optically active lactones (Figure 32).33 A cyclohexanone monooxygenase from Acinetobacter calcoaceticus has been widely used. In the oxidation of... 

Dynamic kinetic resolution process was also applied to biocatalytic Baeyer-Villiger oxidations. The recombinant E. coli expressing the cyclohexanone monooxygenase from A. calcoaceticus was used for the oxidation of racemic... 

Figure 16.5-36. Furstoss model for the active site of cyclohexanone monooxygenase from Acinetobactercalcoaceticus NCIMB 9871.

Figure 16.5-39. Cubic space filling model of the active site of cyclohexanone monooxygenase from Acinetobacter calcoaceticus NCIMB 9871, based on the results of the oxidations of a series of bicyclic ketones. The catalytic oxygen is circled. The main (M) hydrophobic large (HL) and hydrophobic small (Hs) pockets are depicted. The correct arrangements of the Criegee intermediate are also shown.

The (S)-(-)-sulfoxide is predominantly produced (82 % S, 18 % R) from p-tolyl ethyl sulfide when cyclohexanone monooxygenase from Acinetobacter sp. NCIB 9871191 was used, whereas the the FAD-containing monooxygenase from hog liver micro-somes oxidizes p-tolyl ethyl sulfide to yield the (R)-(+)-sulfoxide enantiomer as the major product (95 % R, 5 % S) 15). 

The mechanisms of a few Baeyer-Villiger monooxygenases have been studied in detail. The catalytic cycles of cyclohexanone monooxygenase from Acinetobacter NCIB 9871 and phenylacetone monooxygenase from Thermobifida fusca are similar to each other and to that of As with FMO, wasteful and toxic... 

Reetz et al. used this approach to adapt the cyclohexanone monooxygenase from Acinetobacter sp. NCIMB 9871 (EC 1.14.13.22) to the desymmetrization of... 

A systematic study of the sulfoxidation by cyclohexanone monooxygenase from Acinetobacter using as the substrates many alkyl aryl sulfides, dialkyl sulfides and dialkyl disulfides has been carried out by Carrea, Colonna, and colleagues in the presence of NADP and a NADPH-regenerating system [143,144]. Chemical yields are good (at 0.8 mmol scale), with wide variations of ee s (from 0 to 98%) according to the structure of the sulfides. 

In 1991, the group of Willetts [13] published one of the first smart combinations of two redox enzymes for the oxidation of a secondary alcohol mediated by an alcohol dehydrogenase (ADH) from Thermoanaerobium brockii and the subsequent Baeyer-Villiger oxidation mediated by the cyclohexanone monooxygenase from Acinetobacter calcoaceticus NCIMB 9871) of the intermediate ketone... 

Mono oxygenases have been used in Baeyer-Villiger oxidations to obtain optically active lactones (Fig. 10.18). A cyclohexanone monooxygenase from Acmetobacter calcoaceticus has been widely used. In the oxidation of2-oxabicyclo [3.2.0] -heptan-7-oneby A. calcoaceticus (Fig. 10.18(a), n = 0, m = 2), the S,S-substrate led to the normal lactone, whereas the R,R-substrate gave the abnormal lactone, with ee s of 90 and >98%, respectively. Other substrates proceeded with a similar stereochemical outcome. 

Diastereoselective Baeyer-Villiger Oxidation of a 4-Methylenecyclohexanone 87 Using Cyclohexanone Monooxygenase from Acinetobacter on Lab Scale (300 mg)... 

Cyclohexanone monooxygenase from Acinetobacter calcoaceticus NC3B 9871 is the most studied and applied BVMO. It has been demonstrated that this bacterial enzyme is an extremely versatile biocatalyst with an exceptionally broad substrate acceptance. CHMO.. has been employed in himdreds of oxida-tion procedures [26]. In fact, is a well known catalyst in the synthesis of... 

SCHEME 36.15. Regiodivergent BVO of bicyclo[3.2.0]hept-2-ene-6-one 38 using cyclohexanone monooxygenase from A. calcoaceticus NCIMB 9871. ... 

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