Substrate ionization energy influences the epoxidation of m-substituted styrenes catalyzed by chloroperoxidase from Caldariomyces fumago

Muñoz-Guerrero, Fabio A.; Águila, Sergio; Vázquez-Duhalt, Rafael; Campos, Cristian H.; Torres, Cecilia C.; Alderete, Joel B.

doi:10.1016/j.catcom.2016.01.017

Cited by 8 publications

(3 citation statements)

References 26 publications

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“…Along with its native function of halogenating organic substrates using chloride, bromide and iodide ions [ 2 , 3 , 4 ], CPO is also capable of many promiscuous activities, including peroxidase, catalase and cytochrome P450 (P450) types of reactions [ 1 ]. CPO-catalyzed reactions are of biotechnological and environmental importance [ 5 ], therefore attracting current research interest on both the experimental [ 6 , 7 , 8 , 9 , 10 , 11 , 12 , 13 , 14 ] and theoretical sides [ 15 , 16 , 17 , 18 , 19 , 20 , 21 ]. The catalytic cycle requires a two-electron oxidation of the ferric heme center, using hydrogen peroxide or other suitable peroxide, and the glutamic acid side chain (E 183 ) in the distal pocket as a general acid-base catalyst, to form Compound I (CPO-I), a highly reactive oxyferryl porphyrin π-cation radical intermediate [ 15 , 20 , 22 , 23 ].…”

Section: Introductionmentioning

confidence: 99%

How the Proximal Pocket May Influence the Enantiospecificities of Chloroperoxidase-Catalyzed Epoxidations of Olefins

Morozov

Chatfield

2016

IJMS

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Chloroperoxidase-catalyzed enantiospecific epoxidations of olefins are of significant biotechnological interest. Typical enantiomeric excesses are in the range of 66%–97% and translate into free energy differences on the order of 1 kcal/mol. These differences are generally attributed to the effect of the distal pocket. In this paper, we show that the influence of the proximal pocket on the electron transfer mechanism in the rate-limiting event may be just as significant for a quantitatively accurate account of the experimentally-measured enantiospecificities.

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Section: Introductionmentioning

confidence: 99%

How the Proximal Pocket May Influence the Enantiospecificities of Chloroperoxidase-Catalyzed Epoxidations of Olefins

Morozov

Chatfield

2016

IJMS

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“…吸附法 [7,8] [19] , 目前被认为是过氧化物酶家族中催化活性最广泛的酶之一, 因此 CPO 的应用范围非常广, 尤其是在不对称有机合成 [20,21] 以及环境污染物降解 [22,23] 等方面的应用引人瞩目. 衍射峰位相同, 也与文献报道的特征衍射峰相符(2θ＝ 7.4°、12.7°、18.0°) [25] .…”

Section: 引言unclassified

Immobilization of Chloroperoxidase in Metal Organic Framework and Its Catalytic Performance

Zhao¹,

Hu²,

Li³

et al. 2017

Acta Chim. Sinica

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A rapid and efficient preparation of CPO@ZIF-8 by "one pot " method at 30 ℃ in aqueous solution is presented in this paper. The structure of zeolitic imidazolate frameworks (ZIF-8) was constructed while chloroperoxidase (CPO) was incorporated into the channel. Mild reaction conditions ensure maintaining the enzyme activity in the preparation of immobilized CPO. The synthesis of CPO@ZIF-8 was performed by mixing zinc nitrate solution and polyvinylpyrrolidone solution (PVP, M w : 10000, 10 mg/mL, 400 μL), chloroperoxidase (CPO) (0.214 mmol/L, 500 μL) and 2-methylimidazole (1.25 mol/L, 25 mL) and stirring for 15 min at 30 ℃, followed by washing and centrifuging for 3 cycles at 4 ℃ for 8 min. The structure of CPO@ZIF-8 was characterized by scanning electron microscope (SEM), transmission electron microscopy (TEM) and X-ray diffraction (XRD), indicating that the incorporation of enzyme molecules did not affect the crystal structure of ZIF-8. To further confirm the incorporation of enzyme into ZIF-8, CPO was labeled by fluorescent probes fluorescein isothiocyanate (FITC) and subjected to the same procedure to synthesize the FITC-CPO@ZIF-8. Confocal laser scanning microscopy (CLSM) proved that CPO was distributed evenly and embedded in the whole framework of CPO@ZIF-8. Compared with the method of preparing ZIF-8 firstly, and then immobilizing enzyme molecule by physical adsorption, the immobilization efficiency of enzyme was enhanced by introducing the enzyme into the whole framework, moreover, the catalytic efficiency of the immobilized CPO was increased due to high specific surface area of ZIF-8. The catalytic performance of the CPO@ZIF-8 was evaluated by the conversion rate of 2,2'-azinobis-(3-ethylbenzthiazoline-6-sulphonate) (ABTS). The rigid shielding environment provided by the three-dimensional channel of ZIF-8 effectively improved the thermal stability, pH stability, and tolerance to organic solvents of the CPO@ZIF-8 under harsh reaction conditions compared with the free enzyme. When incubated at 50 ℃, 60 ℃, 70 ℃, 80 ℃ and 90 ℃ for 1 h, 97.1%, 87.8%, 80.2%, 68.1% and 41.5% of the activity of CPO@ZIF-8 were reserved. When incubated at 50 ℃, 60 ℃, 70 ℃ and 80 ℃ for 3 h, there were still 91.4%, 77.8%, 64.7% and 50.3% of the activity remained. The tolerance of CPO@ZIF-8 to organic solvent DMF, methanol and methyl cyanide was enhanced to 30%～40%.

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“…Chloroperoxidase (CPO), a heme-thiolate protein secreted by the marine fungus Caldariomyces fumago, is recognized as a versatile catalyst for various organic transformations including halogenation, Materials and Design 111 (2016) [414][415][416][417][418][419][420] oxidation, peroxidation, epoxidation and hydroxylation with high enantioselectivity [1][2][3][4]. However, the use of CPO in large-scale industrial applications is often handicapped by a lack of long-term operational stability, difficult recovery and the inability to be recycled [5].…”

Section: Introductionmentioning

confidence: 99%

Bienzymatic nanoreactors composed of chloroperoxidase–glucose oxidase on Au@Fe3O4 nanoparticles: Dependence of catalytic performance on the bioarchitecture

Gao

Jiang

et al. 2016

Materials & Design

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Substrate ionization energy influences the epoxidation of m-substituted styrenes catalyzed by chloroperoxidase from Caldariomyces fumago

Cited by 8 publications

References 26 publications

How the Proximal Pocket May Influence the Enantiospecificities of Chloroperoxidase-Catalyzed Epoxidations of Olefins

How the Proximal Pocket May Influence the Enantiospecificities of Chloroperoxidase-Catalyzed Epoxidations of Olefins

Immobilization of Chloroperoxidase in Metal Organic Framework and Its Catalytic Performance

Bienzymatic nanoreactors composed of chloroperoxidase–glucose oxidase on Au@Fe3O4 nanoparticles: Dependence of catalytic performance on the bioarchitecture

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