Differential substrate behaviour of phenol and aniline derivatives during conversion by horseradish peroxidase

Haandel, M.J.H. van; Claassens, Margo M. J.; Hout, N. van der; Boersma, Marelle G.; Vervoort, Jacques; Rietjens, Ivonne M. C. M.

doi:10.1016/s0167-4838(99)00199-5

Cited by 29 publications

(15 citation statements)

References 19 publications

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“…The oxidation rate of phenols with the cpd II complex was shown to be higher by 1-3 orders of mag nitude as compared to anilines provided that ioniza tion potentials were similar [7,9].…”

Section: Resultsmentioning

confidence: 98%

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Quantitative correlations relating the interaction of Zn(II)-tetraphenylporphine and horseradish peroxidase with amines

Andreev

Sobolev

2012

Russ J Bioorg Chem

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Reactions ofnucleophilic substitution and enzymatic processes with participation of metal-porphyrins (MP) are considered from the point of view of Zn-tetraphenylporphin (Zn-TPhP) coordination with corresponding ligand/nucleophyl/substrate/base. Linear correlations perform between kinetic parameters of process of coordination of Zn-TPhP in chloroform (constants of stability) and reactions of nucleophilic substitution both in aqueous and organic solvents with participation ofpyridines, N-oxides ofpyridines, anilines, primary amines and oxidation of anilines by horseradish peroxidase in aqueous solutions (rate constants). Thermodynamic parameters of complexation and nucleophilic substitution mutually correlate linearly in the case of pyridines, anilines and primary amines.

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“…The oxidation rate of phenols with the cpd II complex was shown to be higher by 1-3 orders of mag nitude as compared to anilines provided that ioniza tion potentials were similar [7,9].…”

Section: Resultsmentioning

confidence: 98%

“…It is natural that good linear correlations (r > 0.99) are also observed between logarithms of the rate con stants of enzymatic oxidation [9] and nucleophilic substitution [16][17][18].…”

Section: Resultsmentioning

confidence: 99%

Quantitative correlations relating the interaction of Zn(II)-tetraphenylporphine and horseradish peroxidase with amines

Andreev

Sobolev

2012

Russ J Bioorg Chem

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“…Interestingly, unlike reported examples using free peroxidases (HRP), [41] high conversion yields were also achieved when aniline derivatives were assayed. We measured almost complete degradation of 4-aminophenol (98%) and almost complete (93%) or reasonable (67%) degradation of nonphenolic secondary (N-phenyl-p-phenylenediamine) and simple (4-aminobenzoic acid) anilines, respectively ( Figure S25, Supporting Information).…”

Section: Test Of the Degradation Potential Of Inr_3 Samplementioning

confidence: 86%

Nanoconfined (Bio)Catalysts as Efficient Glucose‐Responsive Nanoreactors

Rodriguez‐Abetxuko

Muñumer

Okuda

et al. 2020

Adv Funct Materials

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Herein, the design, synthesis, and characterization of bifunctional hybrid nanoreactors used for concurrent one‐pot chemoenzymatic reactions are shown. In the design, the enzyme, glucose oxidase, is wrapped with a peroxidase‐mimetic catalytic polymer. Hemin, the organic catalyst, is linked to the flexible polymeric scaffold through coordination to the imidazole groups that hang out the network. This spatial arrangement, which works as a metabolic channel, is optimized for cooperative chemoenzymatic reactions in which the enzyme catalyzes first. A deep characterization of the integrated nanoreactors demonstrates that the confinement of two distinct catalytic sites in the nanospace is very effective in one‐pot reactions. Moreover, besides its role as scaffold material, the polymeric mantel protects both the biocatalyst and the chemical catalyst from degradation and inactivation in the presence of organic solvents. Furthermore, the polymeric environment of the nanoreactors can be tailored in order to trigger the assembly of those into highly active heterogeneous hybrid catalysts. Finally, the new nanoreactors are applied to the efficient degradation of organic aromatic compounds using glucose as the only fuel.

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“…HRP is one of the heme peroxidases, which catalyzes different of oxidative transformations of both organic and inorganic substrates in the presence of a reducing compound by hydrogen peroxide (Van Haandel, Claassens, et al, 1999), or alkyl peroxides (Bodtke, Pfeiffer, et al, 2005). HRP also has the capacity to polymerize amines and phenols resulting in polyphenols.…”

Section: The Biochemical Significance Of Hrpmentioning

confidence: 99%

Monitoring the Chemical Hydroxylation of Complex Phenolic Compounds

Samrgandi¹

2021

Preprint

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It might be industrially or bio-medically important to confirm and monitor the hydroxylation of phenolic amine substrates via mass spectrometry. Phenolic amines may be assayed by colorimetric reactions, liquid chromatography (LC) or thin layer chromatography (TLC), spectrophotometry (UV VIS) or other methods that may not confirm the product molecule with reasonable specificity. Phenolic amine compounds may easily enter the gas phase by electrospray ionization (ESI) and the compounds parent and subsequent fragment ions examined by tandem mass spectrometry (MS/MS). Thus a number of phenolic amine or other reaction products might be monitored and confirmed by liquid chromatography with electrospray ionization and tandem mass spectrometry (LC-ESI-MS/MS). L-tyrosine was reacted with dihydroxyfumaric acid (DHFA) at 0 °C in the presence of bubbling O2 in 400 mL flask respectively or ≥ 100 μL volume in a 96 well plate in an oxygen atmosphere resulting in the product L-DOPA (L-3,4 dihydroxyphenylalanine). The production of L-DOPA was examined with nitrite-molybdate in 0.5 M HCl followed the addition of 1 M of NaOH to form a red color quantified by absorbance at 510 nm. Thin layer chromatography with staining for amines by ninhydrin was used to detect the production of LDOPA. LC-ESI-MS/MS confirmed the molecular identity of the L-DOPA product with a parent ion predominately observed at an m/z value of 198 [M+1H] and the major fragment ions at 181m/z and 151m/z. Monitoring the 181 m/z fragment ion permitted the quantification of L-DOPA over time to ≤1 pM in the reaction vessel with respect to external standards. The hydroxylation of tyrosine was observed to require O2 and DHFA and produced a strong yield at pH 2 but was not dependent on Horseradish peroxidase (HRP) and proceeded in the presence of EDTA. The hydroxylation reaction of tyrosine was depending on DHFA, oxygen and acid (DOA).We conclude that DOA hydroxylation by LC-ESI-MS/MS may be directly applicable to monitoring the industrial modification of a wide class of phenolic amines.

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Differential substrate behaviour of phenol and aniline derivatives during conversion by horseradish peroxidase

Cited by 29 publications

References 19 publications

Quantitative correlations relating the interaction of Zn(II)-tetraphenylporphine and horseradish peroxidase with amines

Quantitative correlations relating the interaction of Zn(II)-tetraphenylporphine and horseradish peroxidase with amines

Nanoconfined (Bio)Catalysts as Efficient Glucose‐Responsive Nanoreactors

Monitoring the Chemical Hydroxylation of Complex Phenolic Compounds

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