Chloroperoxidase

Thomas, John A.; Morris, David R.; Hager, Lowell P.

doi:10.1016/s0021-9258(18)63032-7

Cited by 208 publications

(42 citation statements)

References 15 publications

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“…and with concentrations of CLP and H 2 O 2 used in this work one arrives at k 1 % 10 5 m À1 s À1 , which is comparable with the rate constant reported previously of 1.1 Â 10 5 m À1 s À1 (pH 3.4). [35] This coincidence also suggests that k 1 refers to rate-limiting steps and the simplest scheme to account for the kinetics observed is given by Equations ( 1) and (2).…”

Section: Clp-catalyzed Oxidation Of Alkylferrocenes By H 2 Omentioning

confidence: 83%

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Enantioselectivity in Enzyme-Catalyzed Electron Transfer to and from Planar Chiral Organometallic Compounds

et al. 1998

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/k(R)-1 are 1.7 and 1.6, respectively. Based on the known X-ray structural data for the active site of GO, it has been tentatively suggested that the enantioselectivity originates from the hydrophobic contact between the enzyme tyr-68 residue and the h 5 -C 5 H 5 ring of 1 , and a hydrogen bond network formed by his-516 and/or his-559 residues and the carboxylic group of the ferrocene derivative. The findings reported confirm the existence of enantioselective electron transfer between oxidoreductases and organometallic compounds with a planar chirality. The lack of kinetic enantioselectivity may be a result of i) the incorrect ratelimiting step, ii) unfavorable pH region, and iii) the deficit of charged groups attached to ferrocenes.

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Section: Clp-catalyzed Oxidation Of Alkylferrocenes By H 2 Omentioning

confidence: 83%

“…Precedents for such a mechanism exist in the literature, [34] and an estimate for k 1 is available. [35] Assuming that k 1 is rate-limiting, it follows that…”

Section: Clp-catalyzed Oxidation Of Alkylferrocenes By H 2 Omentioning

confidence: 99%

Enantioselectivity in Enzyme-Catalyzed Electron Transfer to and from Planar Chiral Organometallic Compounds

et al. 1998

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“…The figures were made using DIAMOND 31 software. Crystallographic data (excluding structure factors) for the structure reported here have been deposited with the Cambridge Crystallographic Data Centre, as supplementary publication numbers CCDC 902422 (1) and 972967 (2).…”

Section: Methodsmentioning

confidence: 99%

“…Catalases are enzymes that protect cells from deleterious effects caused by hydrogen peroxide. Besides heme-type catalases 1 and particular enzymes such as chloroperoxidase 2 that disproportionate hydrogen peroxide in addition to their peroxidase activity, there is a class of manganese catalases that can be found in bacterial organisms such as Lactobacillus plantarum, 3 Thermus thermophilus, 4 and Thermoleophilum album. 5 These enzymes are an extremely effective defence against 'oxidative stress' since they convert hydrogen peroxide into water and oxygen.…”

Section: Introductionmentioning

confidence: 99%

Effective catalytic disproportionation of aqueous H₂O₂with di- and mono-nuclear manganese(ii) complexes containing pyridine alcohol ligands

et al. 2014

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The two novel manganese(II) complexes with 2-hydroxymethylpyridine (2-CH2OHpy) {[Mn2(μ-Cl)2(2-CH2OHpy)4]Cl2·2H2O (1)} and 2-hydroxyethylpyridine (2-(CH2)2OHpy) {[Mn(2-(CH2)2OHpy)2(NCS)2] (2)} were synthesized and characterized by means of X-ray diffraction, IR, EPR, HF EPR spectroscopy, magnetic and TG/DTG data. The complexes show catalase-like activity in neutral aqueous solution since they were able to disproportionate H2O2 to harmless H2O and O2. Both complexes act as true catalysts since they reverted to their original form after depleting all the H2O2, as suggested by the operando resonant inelastic X-ray spectroscopy (RIXS) measurements.

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“…At pH 5 or above the halogenating activity of CPO is lost but the enzyme is still active in the oxidation of various substrates, which is our reaction of interest. 35,39,40 The CPO-polymersome (CP) activity was measured as the rate of oxidation of pyrogallol to purpurogallin (Scheme 1). 41 The oxidation activity apparently was not affected by the presence of THF.…”

Section: Encapsulation Of Chloroperoxidasementioning

confidence: 99%

Biocatalytic oxidation by chloroperoxidase from Caldariomyces fumago in polymersome nanoreactors

et al. 2009

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The encapsulation of chloroperoxidase from Caldariomyces fumago (CPO) in block copolymer polymersomes is reported. Fluorescence and electron microscopy show that when the encapsulating conditions favour self-assembly of the block copolymer, the enzyme is incorporated with concentrations that are 50 times higher than the enzyme concentration before encapsulation. The oxidation of two substrates by the encapsulated enzyme was studied: i) pyrogallol, a common substrate used to assay CPO enzymatic activity and ii) thioanisole, of which the product, (R)-methyl phenyl sulfoxide, is an important pharmaceutical intermediate. The CPO-loaded polymersomes showed distinct reactivity towards these substrates. While the oxidation of pyrogallol was limited by diffusion of the substrate into the polymersome, the rate-limiting step for the oxidation of thioansiole was the turnover by the enzyme.

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Chloroperoxidase

Cited by 208 publications

References 15 publications

Enantioselectivity in Enzyme-Catalyzed Electron Transfer to and from Planar Chiral Organometallic Compounds

Enantioselectivity in Enzyme-Catalyzed Electron Transfer to and from Planar Chiral Organometallic Compounds

Effective catalytic disproportionation of aqueous H₂O₂with di- and mono-nuclear manganese(ii) complexes containing pyridine alcohol ligands

Biocatalytic oxidation by chloroperoxidase from Caldariomyces fumago in polymersome nanoreactors

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Chloroperoxidase

Cited by 208 publications

References 15 publications

Enantioselectivity in Enzyme-Catalyzed Electron Transfer to and from Planar Chiral Organometallic Compounds

Enantioselectivity in Enzyme-Catalyzed Electron Transfer to and from Planar Chiral Organometallic Compounds

Effective catalytic disproportionation of aqueous H2O2with di- and mono-nuclear manganese(ii) complexes containing pyridine alcohol ligands

Biocatalytic oxidation by chloroperoxidase from Caldariomyces fumago in polymersome nanoreactors

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Effective catalytic disproportionation of aqueous H₂O₂with di- and mono-nuclear manganese(ii) complexes containing pyridine alcohol ligands