Stereospecific Sulfoxidation by Toluene and Naphthalene Dioxygenases

Lee, Kyoung; Brand, J. M.; Gibson, David T.

doi:10.1006/bbrc.1995.1928

Cited by 73 publications

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“…TDO is a versatile enzyme, mechanistically. It can catalyze monooxygenation (23,31), desaturation (28), O dealkylation (22), N dealkylation (12), sulfoxidation (12), and oxidative dehalogenation (14,30) reactions.…”

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Oxidation of aliphatic olefins by toluene dioxygenase: enzyme rates and product identification

Lange

Wackett

1997

J Bacteriol

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Toluene dioxygenase from Pseudomonas putida F1 has been studied extensively with aromatic substrates. The present work examined the toluene dioxygenase-catalyzed oxidation of various halogenated ethenes, propenes, butenes and nonhalogenated cis-2-pentene, an isomeric mix of 2-hexenes, cis-2-heptene, and cis-2-octene as substrates for toluene dioxygenase. Enzyme specific activities were determined for the more water-soluble C 2 to C 5 compounds and ranged from <4 to 52 nmol per min per mg of protein. Trichloroethene was oxidized at a rate of 33 nmol per min per mg of protein. Products from enzyme reactions were identified by gas chromatography-mass spectrometry. Proton and carbon nuclear magnetic resonance spectroscopy of compounds from whole-cell incubation confirmed the identity of products. Substrates lacking a halogen substituent on sp 2 carbon atoms were dioxygenated, while those with halogen and one or more unsubstituted allylic methyl groups were monooxygenated to yield allylic alcohols. 2,3-Dichloro-1-propene, containing both a halogenated double bond and a halogenated allylic methyl group, underwent monooxygenation with allylic rearrangement to yield an isomeric mixture of cis-and trans-2,3-dichloro-2-propene-1-ol.Toluene dioxygenase (TDO) is a multicomponent enzyme system from Pseudomonas putida F1 (32) which catalyzes the dioxygenation of toluene to (ϩ)-cis-1S,2R-dihydroxy-3-methylcyclohexa-3,5-diene (toluene cis-dihydrodiol), initiating toluene metabolism to tricarboxylic acid cycle intermediates (8). The TDO enzyme system components have been purified (25-27), and its genes have been cloned, sequenced, and expressed in Escherichia coli (33). Over 130 substrates are oxidized by TDO and a small set of closely related enzymes (9). TDO is a versatile enzyme, mechanistically. It can catalyze monooxygenation (23, 31), desaturation (28), O dealkylation (22), N dealkylation (12), sulfoxidation (12), and oxidative dehalogenation (14, 30) reactions.TDO oxidizes trichloroethene (TCE) (30), a common groundwater pollutant. In mammals, TCE can be oxidized to reactive intermediates, via reactions catalyzed by hepatic cytochrome P-450s (19). Also, in groundwater, TCE can sometimes undergo reductive dehalogenation to vinyl chloride, a potent human carcinogen (29). This necessitates its removal from contaminated sites via the use of remediation technologies (4). A knowledge of the products generated via biological oxidation of pollutants is essential for determining the feasibility of bioremediation. For example, TDO oxidizes TCE to two completely nonchlorinated products, glyoxylate and formate (14). The mechanism proposed to explain the product data invoked an enzyme-bound dioxygenated intermediate that rearranged to the observed products. The mechanistic path could only be inferred, and it is of interest to further explore the oxidation of substrates structurally related to TCE.The class of C 3 to C 8 alkenes have been studied little as TDO substrates in comparison to aromatic compounds and halogenated ethenes. In t...

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Oxidation of aliphatic olefins by toluene dioxygenase: enzyme rates and product identification

Lange

Wackett

1997

J Bacteriol

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“…1). Recent studies have shown that NDO exhibits a relaxed substrate specificity and catalyzes multiple oxidative reactions which lead to stereospecific monohydroxylation (9,24,31), desaturation (9,23,29), stereospecific sulfoxidation (18), O dealkylation (23), and N dealkylation (19) with appropriate substrates.…”

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“…The rate of formation of 1-phenyl-1,2-ethanediol was determined by dioxygen consumption and NADH oxidation. Dioxygen consumption was measured with a Clark-type oxygen electrode (Rank Brothers, Cambridge, England) as previously described (18). Reaction mixtures contained, in 1.0 ml of 50 mM MES buffer, pH 6.…”

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Stereospecific dihydroxylation of the styrene vinyl group by purified naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816-4

Lee

Gibson

1996

J Bacteriol

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Naphthalene dioxygenase (NDO) from Pseudomonas sp. strain NCIB 9816-4 adds both atoms of the dioxygen molecule to styrene to form (R)-1-phenyl-1,2-ethanediol. Product formation is tightly coupled to dioxygen consumption and NADH oxidation. NDO oxidizes styrene-d 8 at almost the same initial rate as styrene. The results indicate that dioxygen activation by NDO is different from that by cytochrome P-450 and other monooxygenases, which oxidize styrene to styrene 1,2-oxide.Bacterial dioxygenases which contain non-heme iron and Rieske-type (2Fe-2S) redox clusters play a crucial role in the initiation of the degradation of many aromatic hydrocarbons. These enzymes add both atoms of the dioxygen molecule to the aromatic ring of the substrate to form cis-dihydrodiols (10). One well-known example is the three-component naphthalene dioxygenase (NDO) from Pseudomonas sp. strain NCIB 9816-4 (6, 7, 11, 12, 26, 27), which catalyzes the homochiral dihydroxylation of naphthalene to (ϩ)-cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene (cis-naphthalene dihydrodiol) in the presence of dioxygen and NAD(P)H (15, 16) ( Fig. 1). Recent studies have shown that NDO exhibits a relaxed substrate specificity and catalyzes multiple oxidative reactions which lead to stereospecific monohydroxylation (9, 24, 31), desaturation (9, 23, 29), stereospecific sulfoxidation (18), O dealkylation (23), and N dealkylation (19) with appropriate substrates.Almost all of the reactions catalyzed by NDO are also catalyzed by cytochrome P-450 (hereafter called P-450). However, P-450 has not been reported to form cis-dihydrodiols and NDO has not been reported to form epoxides or catalyze National Institutes of Health shift reactions (5). We used styrene as a substrate for NDO to probe for epoxide formation, since P-450 monooxygenases are known to oxidize styrene to styrene 1,2-oxide (8, 34).Identification of reaction products. The oxidation of styrene by purified NDO components (reductase NAP , ferredoxin NAP , and ISP NAP ) (19, 28) was conducted in 2 ml of 50 mM sodium 2-(N-morpholino)ethanesulfonate (MES) buffer, pH 6.8, containing NADH (0.5 mol), Reductase NAP (16 g), Ferredoxin NAP (35 g), ISP NAP (50 g), Fe(NH 4 ) 2 (SO 4 ) 2 ⅐ 6H 2 O (0.1 mol), and styrene (0.25 mol). After 2 h, an internal standard (25 l of a 10 mM methanol stock solution of 1-phenethyl alcohol) was added to the reaction mixture, which was then extracted with ethyl acetate, concentrated, and analyzed by gas chromatography-mass spectrometry as described previously (24). Only one product, which eluted at 10.72 min and gave a mass spectrum identical to that given by authentic 1-phenyl-1,2-ethanediol, was detected. This product was purified by thin-layer chromatography (solvent, chloroform-acetone ϭ 8:2, R f ϭ 0.19), and its enantiomeric composition was determined by chiral stationary-phase-high-performance liquid chromatography (HPLC) on a Chiralcel OB-H column (4.6 mm by 25 cm, 5-m particle size; Chiral Technologies Inc., Exton, Pa.) (24). Enantiomers were eluted with hexane and 2-propanol ...

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“…178 Pseudomonas putida NCIB 9816-4, which expresses the enzyme naphthalene dioxygenase, was used to prepare a variety of enantioenriched aryl alkyl sulfoxides with up to 98% ee being reported. 179 Biocatalytic sulfoxidation using the topsoil bacterium Pseudomonas frederiksbergensis has been reported by Adam et al 180 For example 8, was obtained effectively enantiopure (> 99% ee)…”

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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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Stereospecific Sulfoxidation by Toluene and Naphthalene Dioxygenases

Cited by 73 publications

References 0 publications

Oxidation of aliphatic olefins by toluene dioxygenase: enzyme rates and product identification

Oxidation of aliphatic olefins by toluene dioxygenase: enzyme rates and product identification

Stereospecific dihydroxylation of the styrene vinyl group by purified naphthalene dioxygenase from Pseudomonas sp. strain NCIB 9816-4

Synthesis of enantioenriched sulfoxides

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