The use of cyclohexa-3,5-diene-1,2-diols in enantiospecific synthesis

Carless, H. A. J.

doi:10.1016/s0957-4166(00)82174-6

Cited by 218 publications

(68 citation statements)

References 55 publications

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“…Because of its broad specificity towards a wide range of aromatic hydrocarbons, NDO can produce chiral petrochemical-based precursors for the synthesis of specialty chemicals (70,216,509,510). Chiral cyclohexadiene diols are potential precursors for the enantiospecific synthesis of many bioactive molecules, and toluene dioxygenase has been used for biosynthesis of enantiomers of erythrose (78,99,266,555,665). cis-Chlorodihydrodiol is an extremely versatile synthon (265).…”

Section: Enzymatic Upgrading Of Petroleum Fractions and Pure Hydrocarmentioning

confidence: 99%

Recent Advances in Petroleum Microbiology

Hamme¹,

Singh

Ward

2003

Microbiol Mol Biol Rev

1,201

640

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Recent advances in molecular biology have extended our understanding of the metabolic processes related to microbial transformation of petroleum hydrocarbons. The physiological responses of microorganisms to the presence of hydrocarbons, including cell surface alterations and adaptive mechanisms for uptake and efflux of these substrates, have been characterized. New molecular techniques have enhanced our ability to investigate the dynamics of microbial communities in petroleum-impacted ecosystems. By establishing conditions which maximize rates and extents of microbial growth, hydrocarbon access, and transformation, highly accelerated and bioreactor-based petroleum waste degradation processes have been implemented. Biofilters capable of removing and biodegrading volatile petroleum contaminants in air streams with short substrate-microbe contact times (<60 s) are being used effectively. Microbes are being injected into partially spent petroleum reservoirs to enhance oil recovery. However, these microbial processes have not exhibited consistent and effective performance, primarily because of our inability to control conditions in the subsurface environment. Microbes may be exploited to break stable oilfield emulsions to produce pipeline quality oil. There is interest in replacing physical oil desulfurization processes with biodesulfurization methods through promotion of selective sulfur removal without degradation of associated carbon moieties. However, since microbes require an environment containing some water, a two-phase oil-water system must be established to optimize contact between the microbes and the hydrocarbon, and such an emulsion is not easily created with viscous crude oil. This challenge may be circumvented by application of the technology to more refined gasoline and diesel substrates, where aqueous-hydrocarbon emulsions are more easily generated. Molecular approaches are being used to broaden the substrate specificity and increase the rates and extents of desulfurization. Bacterial processes are being commercialized for removal of H2S and sulfoxides from petrochemical waste streams. Microbes also have potential for use in removal of nitrogen from crude oil leading to reduced nitric oxide emissions provided that technical problems similar to those experienced in biodesulfurization can be solved. Enzymes are being exploited to produce added-value products from petroleum substrates, and bacterial biosensors are being used to analyze petroleum-contaminated environments

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Section: Enzymatic Upgrading Of Petroleum Fractions and Pure Hydrocarmentioning

confidence: 99%

Recent Advances in Petroleum Microbiology

Hamme¹,

Singh

Ward

2003

Microbiol Mol Biol Rev

1,201

640

View full text Add to dashboard Cite

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“…The use of dioxygenases to initiate biocatalytic routes for the production of pharmaceuticals and natural products has received significant attention of late (9,12,25,42), and the possibility of generating new synthons with opposite stereochemistry is an attractive alternative to asymmetric chemical synthesis (7).…”

Section: Pseudomonas Putida F1 Was Used To Produce Enantiomerically Pmentioning

confidence: 99%

Regioselectivity and Enantioselectivity of Naphthalene Dioxygenase during Arene cis -Dihydroxylation: Control by Phenylalanine 352 in the α Subunit

et al. 2000

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The naphthalene dioxygenase (NDO) system catalyzes the first step in the degradation of naphthalene by Pseudomonas sp. strain NCIB 9816-4. The enzyme has a broad substrate range and catalyzes several types of reactions including cis-dihydroxylation, monooxygenation, and desaturation. Substitution of valine or leucine at Phe-352 near the active site iron in the ␣ subunit of NDO altered the stereochemistry of naphthalene cis-dihydrodiol formed from naphthalene and also changed the region of oxidation of biphenyl and phenanthrene. In this study, we replaced Phe-352 with glycine, alanine, isoleucine, threonine, tryptophan, and tyrosine and determined the activity with naphthalene, biphenyl, and phenanthrene as substrates. NDO variants F352W and F352Y were marginally active with all substrates tested. F352G and F352A had reduced but significant activity, and F352I, F352T, F352V, and F352L had nearly wild-type activities with respect to naphthalene oxidation. All active enzymes had altered regioselectivity with biphenyl and phenanthrene. In addition, the F352V and F352T variants formed the opposite enantiomer of biphenyl cis-3,4-dihydrodiol [77 and 60% (؊)-(3S,4R), respectively] to that formed by wild-type NDO [>98% (؉)-(3R,4S)]. The F352V mutant enzyme also formed the opposite enantiomer of phenanthrene cis-1,2-dihydrodiol from phenanthrene to that formed by biphenyl dioxygenase from Sphingomonas yanoikuyae B8/36. A recombinant Escherichia coli strain expressing the F352V variant of NDO and the enantioselective toluene cis-dihydrodiol dehydrogenase from Pseudomonas putida F1 was used to produce enantiomerically pure (؊)-biphenyl cis-(3S,4R)-dihydrodiol and (؊)-phenanthrene cis-(1S,2R)-dihydrodiol from biphenyl and phenanthrene, respectively.The naphthalene dioxygenase (NDO) system (EC 1.14.12.12) catalyzes the first step in the degradation of naphthalene in Pseudomonas sp. NCIB 9816-4. In this reaction, both atoms of O 2 are added to the aromatic ring to form (ϩ)-cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene (naphthalene cis-dihydrodiol) (28,29). NDO consists of three components. An iron-sulfur flavoprotein reductase and a Rieske iron-sulfur ferredoxin transfer electrons from NAD(P)H to the catalytic oxygenase component (15,16,21,22). The oxygenase consists of large (␣) and small (␤) subunits that form an ␣ 3 ␤ 3 native structure (31). Each ␣ subunit contains a Rieske [2Fe-2S] center and mononuclear nonheme iron (15, 31). Electrons are transferred from the Rieske center in one ␣ subunit to the mononuclear iron in an adjacent ␣ subunit (31, 39), and this is the site of oxygen activation and catalysis.NDO catalyzes the oxidation of a wide variety of aromatic compounds, and many of the products are enantiomerically pure chiral compounds (9, 24, 45). The use of dioxygenases to initiate biocatalytic routes for the production of pharmaceuticals and natural products has received significant attention of late (9,12,25,42), and the possibility of generating new synthons with opposite stereochemistry is an attractive alternativ...

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“…Other bacterial dioxygenases show similar properties, and more than 130 chiral arene cis-dihydrodiols have been produced from a small number of strains (7,35,48). The high enantiomeric purity of these compounds has led to their use as chiral synthons in the enantiospecific synthesis of a wide variety of biologically active natural products (7,8,46,57). The present studies focus on another facet of this interesting group of dioxygenases, that is, their ability to catalyze reactions other than the formation of arene cis-dihydrodiols.…”

mentioning

confidence: 99%

Desaturation, dioxygenation, and monooxygenation reactions catalyzed by naphthalene dioxygenase from Pseudomonas sp. strain 9816-4

et al. 1995

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Pseudomonas sp. strain 9816-4 grows with naphthalene as the sole source of carbon and energy (9). The initial reaction is catalyzed by a multicomponent enzyme system designated naphthalene dioxygenase (NDO) (11,12,23,24). NDO catalyzes the NAD(P)H-dependent enantiospecific incorporation of dioxygen into naphthalene to form (ϩ)-cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene (cis-naphthalene dihydrodiol) (26, 27) ( Fig. 1). An analogous reaction is catalyzed by toluene dioxygenase (TDO) from Pseudomonas putida F1, where enantiomerically pure (ϩ)-cis-(1S,2R)-dihydroxy-3-methylcyclohexa-3,5-diene (cis-toluene dihydrodiol) is the first detectable oxidation product (17,31,60). TDO also catalyzes the enantiospecific oxidation of naphthalene to (ϩ)-cis-naphthalene dihydrodiol (18,39).In addition to the enantiospecific oxidation of naphthalene and toluene, NDO and TDO from the above strains oxidize many related aromatic compounds to optically active dihydrodiols (10,18,28,30). Other bacterial dioxygenases show similar properties, and more than 130 chiral arene cis-dihydrodiols have been produced from a small number of strains (7,35,48). The high enantiomeric purity of these compounds has led to their use as chiral synthons in the enantiospecific synthesis of a wide variety of biologically active natural products (7,8,46,57). The present studies focus on another facet of this interesting group of dioxygenases, that is, their ability to catalyze reactions other than the formation of arene cis-dihydrodiols. For example, the TDO expressed by P. putida F39/D oxidizes indan to (1R)-indanol and oxidizes indene to cis-(1S,2R)-indandiol and (1S)-indenol (55). Similar reactions have been reported for TDO from P. putida UV4, although the 1-indenol produced by this strain is the (1R)-enantiomer (3, 5).We now report the identification and absolute stereochemistry of the products formed from indan and indene by NDO from Pseudomonas sp. strain 9816-4 and confirm earlier observations on the desaturation of indan to indene by NDO (22). MATERIALS AND METHODSOrganisms. Pseudomonas sp. strain 9816/11 is a mutant which oxidizes naphthalene stoichiometrically to (ϩ)-cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene (40). This organism is a derivative of Pseudomonas sp. strain 9816-4 (9, 59), which harbors the genes for naphthalene catabolism on an 83-kb NAH plasmid designated pDTG1 (45). Pseudomonas sp. strain 9816/C84, a cured strain, was used as a control in experiments with strain 9816/11. Escherichia coli strain JM109 (DE3)[pDTG141] contains the structural genes (nahAaAbAcAd) for NDO in plasmid pT7-5 (50). Expression of NDO in this strain is inducible by the addition of isopropylthiogalactopyranoside (IPTG). E. coli JM109(DE3)[pT7-5] was used as a control in experiments with strain JM109(DE3) [pDTG141].Biotransformation experiments. Strain 9816/11 was grown at 30ЊC in mineral salts basal medium (MSB) (49) with 0.2% (wt/vol) pyruvate as a carbon source in the presence of 0.05% (wt/vol) salicylate or anthranilate. These aromatic acids induce the s...

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The use of cyclohexa-3,5-diene-1,2-diols in enantiospecific synthesis

Cited by 218 publications

References 55 publications

Recent Advances in Petroleum Microbiology

Recent Advances in Petroleum Microbiology

Regioselectivity and Enantioselectivity of Naphthalene Dioxygenase during Arene cis -Dihydroxylation: Control by Phenylalanine 352 in the α Subunit

Desaturation, dioxygenation, and monooxygenation reactions catalyzed by naphthalene dioxygenase from Pseudomonas sp. strain 9816-4

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