Biocatalytic chlorination of aromatic hydrocarbons by chloroperoxidase of Caldariomyces fumago

Vázquez-Duhalt, Rafael; Ayala, Marcela; Márquez-Rocha, Facundo J.

doi:10.1016/s0031-9422(01)00326-0

Cited by 64 publications

(29 citation statements)

References 29 publications

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“…This enzyme has the capability to transform compounds as different in chemical nature as pesticides [27], polycyclic aromatic hydrocarbons [28], azo dyes [29], and sulfur and nitrogen heterocyclic compounds [30,31]. The wide substrate variability of this enzyme makes it a good candidate for studies of the transformation of pharmaceutical micropollutants.…”

Section: Introductionmentioning

confidence: 99%

Chloroperoxidase-Mediated Halogenation of Selected Pharmaceutical Micropollutants

et al. 2018

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Abstract:The oxidation of eight pharmaceutical micropollutants by chloroperoxidase derived from Caldaromyces fumago using hydrogen peroxide as an electron acceptor is reported. All the tested compounds, namely trazadone, sulfamethoxazole, naproxen, tetracycline, estradiol, ketoconazole, ketorolac, and diclofenac, were found to be substrates for oxidation by chloroperoxidase. The respective oxidation products were identified by electrospray ionization-mass spectrometry. All the products contain at least one chloride atom in their structure after the enzymatic oxidation. Degradability experiments indicated that most of the reaction products are more biodegradable than the corresponding unmodified compounds. The enzyme was found to be catalytically active in effluent from a water treatment facility, transforming the micropollutants with high reaction rates and conversions. The enzyme was immobilized in chitosan macrospheres, which allowed the catalyst to be recycled for up to three treatment cycles in simulated samples of treated residual water. The conversion was high in the first two cycles; however, in the third, a 50% reduction in the capacity of the enzyme to oxidize ketorolac was observed. Additionally, immobilization improved the performance of the enzyme over a wider pH range, achieving the conversion of ketorolac at pH 5, while the free enzyme was not active at this pH. Overall, the results of this study suggest that chloroperoxidase represents a powerful potential catalyst in terms of its catalytic activity for the transformation of pharmaceutical micropollutants.

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Section: Introductionmentioning

confidence: 99%

Chloroperoxidase-Mediated Halogenation of Selected Pharmaceutical Micropollutants

et al. 2018

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“…Methoxychlor (MXC), a synthetic pesticide, has been used as a replacement for DDT and is considered to be a xenoestrogen that disrupts the reproductive system [14]. In addition, 4-alkylphenol ethoxylates (APEs) are widely used as surfactants in lubricant oil addictives, phosphate antioxidants and rubber products [15], and they have been shown to have an estrogenic effect [16]. Furthermore, the metabolites of APEs, such as nonylphenol (NP) and octylphenol (OP), exhibit an estrogenic effect at low concentrations [5,17].…”

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confidence: 99%

Cell Growth of Ovarian Cancer Cells is Stimulated by Xenoestrogens through an Estrogen-Dependent Pathway, but Their Stimulation of Cell Growth Appears not to be Involved in the Activation of the Mitogen-Activated Protein Kinases ERK-1 and p38

Park

Kim

et al. 2009

Journal of Reproduction and Development

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Abstract. Although endocrine disrupting chemicals (EDCs) may interfere with the endocrine system(s) of our body and have estrogenicity or androgenicity, the exact mechanism(s) underlying their detrimental effects is not clearly understood. Thus, in this study, we evaluated the effects of EDCs on proliferation and regulation of transcription of estrogen receptor (ER)-positive BG-1 ovarian cancer cells, and their possible mechanisms were further examined. Treatment with bisphenol A (BPA), nonylphenol (NP), octylphenol (OP) and methoxychlor (MXC) for 24 h resulted in an increase of cell proliferation. Treatment with BPA, NP, OP and MXC increased the estrogen response element (ERE) activity. The increase of cell proliferation and activation of ERE were reversed in the presence of an estrogen receptor antagonist, ICI 182780. These results suggest that ER is involved in EDC-mediated pathway in ovarian cancer cells. Based on this, we further investigated the involvement of EDCs in activation of mitogen-activated protein kinase (MAPK) in relation to cell growth. BPA rapidly induced activation of extracellular signal-regulated kinase (ERK) 1/2 and p38 MAPK at 15 min, but the effect of BPA (10 μM) on stimulation of cell growth was not blocked by pretreatment with inhibitors of MEK (PD98059) or p38 (SB203580) in a dose-dependent manner. Taken together, EDC-induced proliferation is mediated by a genomic effect through ERs and ERE, but EDC-activated MAPK is unlikely to be involved in EDC-induced cell growth in estrogen-responsive ovarian cancer cells. Key words: Endocrine disrupting chemical, Estrogen receptor, Estrogen response element, Extracellular signalregulated kinase, Mitogen-activated protein kinase (J. Reprod. Dev. 55: [23][24][25][26][27][28][29] 2009) varian carcinoma is one of the most frequent gynaecologic cancers, following breast, lung and colorectal cancer [1]. Although the biological causes of ovarian cancer remain unknown, hormonal factors such as estrogen or gonadotropins have been implicated in the etiology of ovarian cancer [2]. In addition, it has been reported that endocrine disrupting chemicals (EDCs) may increase the risk of cancer incidence [3,4]. However, the data associated with the effect of EDCs on ovarian cancer cells are scarce.Since EDCs are known as environmental chemicals that interfere with the hormonal balance of vertebrates and invertebrates, they are considered to be important in physiology and the endocrine system [5,6]. EDCs are released from industrial products such as plastics, pesticides, detergents and other synthetic products. It has been proposed that EDCs may increase human health risks and have potentials to affect the immune system and development of vital organs [7][8][9].Bisphenol-A (BPA), alkylphenols, dichloro-diphenyl-trichloroethane (DDT), polychlorinated biphenyls (PCBs) and phthalates are mainly highlighted among EDCs. BPA, a compound used in polycarbonate and epoxy resins, has been implicated as a potent risk factor for women's health [10]. BPA has been widely use...

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“…These fungi produce extracellular chloroperoxidases (CPOs), heme-or vanadium-containing enzymes that oxidize Cl Ϫ to hypochlorous acid (HOCl) or a similarly reactive chlorine electrophile (18,21). CPOs chlorinate a variety of aromatic substrates (2,15,19,23), but their reactivity with lignin is unknown. We report here that the major structures in lignin are not only chlorinated but also cleaved by the heme CPO of Caldariomyces fumago and the vanadium CPO of Curvularia inaequalis.…”

mentioning

confidence: 99%

Chlorination and Cleavage of Lignin Structures by Fungal Chloroperoxidases

Ortiz-Bermúdez

Srebotnik

Hammel

2003

Appl Environ Microbiol

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Two fungal chloroperoxidases (CPOs), the heme enzyme from Caldariomyces fumago and the vanadium enzyme from Curvularia inaequalis, chlorinated 1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane, a dimeric model compound that represents the major nonphenolic structure in lignin. Both enzymes also cleaved this dimer to give 1-chloro-4-ethoxy-3-methoxybenzene and 1,2-dichloro-4-ethoxy-5-methoxybenzene, and they depolymerized a synthetic guaiacyl lignin. Since fungal CPOs occur in soils and the fungi that produce them are common inhabitants of plant debris, CPOs may have roles in the natural production of high-molecular-weight chloroaromatics and in lignin breakdown.Natural organochlorine compounds are widely distributed in the environment, but the processes that generate them are not completely understood. It is clear that many natural organochlorines are microbial secondary metabolites, whereas others are generated abiotically (22), but little attention has been given to the possibility that biological chlorinations of lignin, the most abundant terrestrial aromatic substance, may produce chloroaromatic compounds. If microbial mechanisms exist to oxidize Cl Ϫ in plant material, the resulting electrophilic chlorine species are likely to react with the electron-rich aromatic rings of lignin (4). This chemistry could explain, in part, why field samples of soil, litter, and decayed wood have all been shown to contain high-molecular-weight chloroaromatics (5,14).Certain plant-pathogenic ascomycetes that are cosmopolitan inhabitants of plant debris provide a possible route for Cl Ϫ oxidation in the vicinity of lignin (6,8,20). These fungi produce extracellular chloroperoxidases (CPOs), heme-or vanadium-containing enzymes that oxidize Cl Ϫ to hypochlorous acid (HOCl) or a similarly reactive chlorine electrophile (18,21). CPOs chlorinate a variety of aromatic substrates (2,15,19,23), but their reactivity with lignin is unknown. We report here that the major structures in lignin are not only chlorinated but also cleaved by the heme CPO of Caldariomyces fumago and the vanadium CPO of Curvularia inaequalis.Chlorination and cleavage of a lignin model dimer. Compound I, 14 C]phenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane (1.0 mCi/mmol), a model of the major nonphenolic arylglycerol-␤-aryl ether structure in lignin (Fig. 1A), was prepared as described previously (9, 12). The model was treated with either commercially available Caldariomyces fumago heme CPO (Sigma) or partially purified Curvularia inaequalis vanadium CPO. The latter enzyme was obtained by DEAE-Sephacel chromatography of the extracellular medium from Curvularia inaequalis cultures (ATCC 10713) as described earlier (17). The reaction mixtures (1.0 ml) contained compound I (3.4 ϫ 10 5 dpm, 160 M), KCl (20 mM), and buffer (25 mM). The buffers were potassium phosphate, pH 3.0, for heme CPO reactions and sodium acetate, pH 4.0, for vanadium CPO reactions. Enzyme was added (35 monochlorodimedone units of heme CPO or 1 monochlorodimedone unit of va...

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Biocatalytic chlorination of aromatic hydrocarbons by chloroperoxidase of Caldariomyces fumago

Cited by 64 publications

References 29 publications

Chloroperoxidase-Mediated Halogenation of Selected Pharmaceutical Micropollutants

Chloroperoxidase-Mediated Halogenation of Selected Pharmaceutical Micropollutants

Cell Growth of Ovarian Cancer Cells is Stimulated by Xenoestrogens through an Estrogen-Dependent Pathway, but Their Stimulation of Cell Growth Appears not to be Involved in the Activation of the Mitogen-Activated Protein Kinases ERK-1 and p38

Chlorination and Cleavage of Lignin Structures by Fungal Chloroperoxidases

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