Chloroperoxidase-catalysed oxidation of alcohols to aldehydes

Kiljunen, Eero; Kanerva, Liisa T.

doi:10.1016/s1381-1177(99)00093-4

Cited by 53 publications

(39 citation statements)

References 25 publications

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“…From a practical point of view however, it is not necessary to have pseudo first order conditions and indeed, it is economically undesirable to have a large excess of one reactant. 60 High substrate concentrations 17,42,67 or the slow addition of peroxide 13,14 can prevent the build-up of excess peroxide which ultimately leads to deactivation indicating that the optimal system involves the addition of peroxide at the rate at which it is consumed 40 . Therefore it should be possible to minimise the effect 65 of solvent-aided deactivation by careful consideration of the reaction conditions.…”

Section: Discussionmentioning

confidence: 99%

“…This may, in part, be attributed to deactivation of the enzymes by the peroxide oxidant at the concentrations required for such reactions [10][11][12] . Strategies to overcome this problem have been developed, including the slow addition 13 or in-situ generation 14 of the peroxide. Alternatively, 30 studies have shown that a high concentration of substrate relative to the peroxide aids the regeneration of the native enzyme and prevents the formation of the peroxidase intermediates which result in enzyme deactivation [15][16][17] .…”

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confidence: 99%

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The effect of solvent on the catalytic properties of microperoxidase-11

O’Reilly

Magner

2011

Phys. Chem. Chem. Phys.

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The effect of a range of solvents on the catalytic oxidation of methyl phenyl sulfide to methyl phenyl sulfoxide by MP-11 and by a cyclodextrin derivative of MP-11 was examined. The addition of low concentrations of alcohols enhanced the initial rate of sulfoxidation rate, most likely due to dispersion of MP-11 aggregates. Higher alcohol concentrations resulted in a decrease in activity arising from solvation of the hydrophobic sulfide, disrupting binding to the catalyst. In alcohols 10 the yield of product was decreased arising from increased rates of MP-11 deactivation via the formation of aldehydes (for primary alcohols) or by peroxide deactivation. The catalytic activity of cyclodextrin modified MP-11 was similar to that of MP-11 itself, demonstrating that it is the Ntermianal side of MP-11 which is the determinant of catalytic activity. Introduction 15The function of enzymes and proteins in non-aqueous solvents has been well established and, in some cases, commercialised [1][2][3][4][5] . Enzyme catalysis and biosensing in organic solvents offers many advantages over aqueous-based processes including increased substrate/analyte solubility, enhanced thermal stability, more 20 favourable reaction thermodynamics, ease of product / biocatalyst recovery and modified selectivity 1,2,[6][7][8][9][10] . The peroxidases are an important group of enzymes which catalyse a wide variety of synthetically useful oxidation reactions using peroxides as oxidants. In spite of this, their potential in non-aqueous catalytic 25 systems has yet to be realised. This may, in part, be attributed to deactivation of the enzymes by the peroxide oxidant at the concentrations required for such reactions [10][11][12] . Strategies to overcome this problem have been developed, including the slow addition 13 or in-situ generation 14 of the peroxide. Alternatively, 30 studies have shown that a high concentration of substrate relative to the peroxide aids the regeneration of the native enzyme and prevents the formation of the peroxidase intermediates which result in enzyme deactivation [15][16][17] . Microperoxidases (MPs) are the products of the proteolytic 35 digestion of cytochrome c. MP-11 contains residues 11 -21 of the parent protein and is prepared by the action of pepsin on cytochrome c. The haem group is covalently attached to the Cys14 and Cys17 residues via sulfide bonds and is coordinated on the proximal side by the imidazole nitrogen of His18. The 6th axial 40 ligand position is either unoccupied or loosely coordinated by water 18 . In this respect the haem configuration is analogous to that of the peroxidase enzymes and MP-11 displays typical peroxidase activity.The array of reactions catalysed by MPs is extensive. The 45 oxidation of phenolic substrates 17,19,20 , peroxide decomposition 21 , sulfide oxidation 22 , Mn 2+ oxidation 23 , the nitration of phenol in the presence of NO 2 -24 , the oxidation of N-methylcarbazole 25 and the dehalogenation of halophenols 26 have all been reported. Thus MPs display activity similar not on...

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

The effect of solvent on the catalytic properties of microperoxidase-11

O’Reilly

Magner

2011

Phys. Chem. Chem. Phys.

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“…Stereoselectivity arises from the fact that to gain access to CPO's active site, the substrates need to properly orient in the channel that connects the surface of the enzyme to the heme pocket. Substrates for these two-electron oxidations include amines, alcohols, aldehydes, alkenes, alkynes, esters, anisoles, sulfides and indoles (111)(112)(115)(116)(117)(118)(119)(120)(121)(122)(123)(124)(125)(126). …”

Section: Two-electron Oxidationsmentioning

confidence: 99%

“…In addition to the reactions described above, CPO is able to catalyze the oxidation of different monoterpenes in the presence of halide to yield halohydrins (167), regio-and stereoselective bromohydration of glycals to produce 2-deoxy-2-bromo saccharides (168), oxidation of unsubstituted and substituted indoles to yield oxindoles (125,169,170), Noxidation of arylamines to give nitroso metabolites (111,169,171), oxidation of alcohols to aldehydes (116), and oxidation of conjugated dienoic esters to yield a variety of products (123). Many of the above compounds can be converted into chemicals that serve as intermediates in the synthesis of flavors, fragrances, and drugs (125,167).…”

Section: Two-electron Oxidationsmentioning

confidence: 99%

The Influence of the Proximal Thiolate Ligand and Hydrogen Bond Network of the Proximal Helix on the Structural and Biochemical Properties of Chloroperoxidase

Shersher¹

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“…Chloroperoxidase (CPO), a heme-thiolate protein secreted by the marine fungus Caldariomyces fumago [23], is a versatile enzyme [25] capable of catalyzing a broad spectrum of chemical reactions including halogenation [28], dehalogenation [39], N-demethylation [37], dismutation [23], epoxidation [42], and oxidation [34,41,129,130,131]. Therefore, CPO has been the subject of numerous biotechnological investigations due to its potential applications in synthetic chemistry as well as pharmaceutical industry [44,46,132,133].…”

Section: Introductionmentioning

confidence: 99%

Nuclear Magnetic Resonance Spectroscopic and Computational Investigations of Chloroperoxidase Catalyzed Regio- and Enantio-Selective Transformations

Zhang¹

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Chloroperoxidase-catalysed oxidation of alcohols to aldehydes

Cited by 53 publications

References 25 publications

The effect of solvent on the catalytic properties of microperoxidase-11

The effect of solvent on the catalytic properties of microperoxidase-11

The Influence of the Proximal Thiolate Ligand and Hydrogen Bond Network of the Proximal Helix on the Structural and Biochemical Properties of Chloroperoxidase

Nuclear Magnetic Resonance Spectroscopic and Computational Investigations of Chloroperoxidase Catalyzed Regio- and Enantio-Selective Transformations

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