Selectivity in the peroxidase catalyzed oxidation of phenolic sulfides

Riso, Antonio De; Gullotti, Michele; Casella, Luigi; Monzani, Enrico; Profumo, Antonella; Gianelli, Luca; Gioia, Luca De; Gaiji, Noura; Colonna, Stefano

doi:10.1016/s1381-1169(03)00321-2

Cited by 10 publications

(3 citation statements)

References 17 publications

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“…4). In this case the simple electron donation from substrate to enzyme is expected in conformity with the experimental study, which show that 4-methylthiophenol behave as a simple phenolic substrate, which react with the oxidative HRP intermediate producing phenoxyl radicals and protons [16].…”

Section: Resultssupporting

confidence: 84%

Modeling the Enantioselective Enzymatic Reaction with Modified Genetic Docking Algorithm

Žiemys,

Rimkutė,

Kulys

2004

NAMC

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The handling algorithms for molecular interaction and docking is of increasing involvement in biological processes modeling. Genetic algorithm, in particular, improves the computation models and leads to more effective and robust calculations. An example of genetic algorithm application for the treatment of enantioselective enzymatic (peroxidase catalyzed) reaction is rendered. The performed modeling revealed the substrate structure influence to the docking in the enzyme active center and provided an explanation to the mechanism of peroxidase-catalyzed asymmetric oxidation reaction. The comparison of modeling results with published experimental data revealed the effectiveness of used algorithm, its suitability for solving problems for enantioselective enzymatic reactions modeling and its relevance to provide the rational design of fine prechiral compounds based targets.

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Section: Resultssupporting

confidence: 84%

Modeling the Enantioselective Enzymatic Reaction with Modified Genetic Docking Algorithm

Žiemys,

Rimkutė,

Kulys

2004

NAMC

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“…Specifically, an energy-minimization algorithm was used to evaluate two intermolecular distances within the enzyme-substrate complex. The first distance, between the phenolic proton and the heme iron, exhibited no correlation with measured reaction rates in this study or two that preceded it (DeRiso et al, 2003;Van Haandel et al, 1996). In contrast, the energy-weighted average distance between the phenolic proton and the purported binding site (dN on HIS42's imidazole ring) (Poulos and Kraut, 1980) was found to be well-correlated with deviation from the E HOMO À ln(k CAT ) trend.…”

Section: Introductioncontrasting

confidence: 70%

Validation of a two‐parameter quantitative structure–activity relationship as a legitimate tool for rational re‐design of horseradish peroxidase

Colosi

Huang

Weber

2007

Biotech & Bioengineering

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Previously reported rates of reaction between six mutant strains of the enzyme horseradish peroxidase (HRP) and a test substrate, 2-methoxyphenol, were found to correlate with characteristic binding distances computed using molecular simulation. The correlation (R(2) = 0.86) bears out a working hypothesis that, based on a quantitative structure-activity relationship (QSAR) we had previously developed for HRP, reductions in binding distances between the HRP enzyme and any selected substrate mediate increased enzyme reactivity towards that substrate. The results validate the use of QSAR as a quantitative means for formulating enzyme mutations designed to achieve enhanced HRP reactivity towards compounds of specific interest.

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“…Incorporation of key descriptors of enzyme−substrate binding features may make the QSAR a more powerful tool to investigate enzymatic reactions. Strategic binding distances can often serve as a convenient quantitative parametrization of the spatial conformation of enzyme−substrate complexes. , van Haandel and de Riso have both tried to correlate HRP-mediated reaction rates to NMR-measured distances between the substrate proton and the heme iron.…”

Section: Introductionmentioning

confidence: 99%

Quantitative Structure−Activity Relationship Based Quantification of the Impacts of Enzyme−Substrate Binding on Rates of Peroxidase-Mediated Reactions of Estrogenic Phenolic Chemicals

2006

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The initial rates of horseradish peroxidase (HRP)-mediated enzymatic reactions of 15 assorted aqueous phase phenolic chemicals were studied. The associated reaction rate constants were found to correlate quantitatively with two independent variables: the highest-occupied molecular orbital energy (E(HOMO)) defining the intrinsic redox reactivities of the phenolic substrates and the distance between a substrate and the deltaN of HIS42's imidazole ring in an HRP/substrate binding complex, obtained through molecular simulations. Highly correlated quantitative structure-activity relationship (QSAR) equations were thus developed. This work provides insights into the impacts that HRP/substrate binding may have on HRP-mediated reactions. Additionally, the QSAR equations developed in the work may serve as a basis to further explore the potential use of HRP-mediated reactions in the treatment of estrogenic contaminants, and they constitute an important tool for redesign and screening of potential proteomic modifications to the wild-type HRP structure intended to enhance reactivity toward selected substrates.

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Selectivity in the peroxidase catalyzed oxidation of phenolic sulfides

Cited by 10 publications

References 17 publications

Modeling the Enantioselective Enzymatic Reaction with Modified Genetic Docking Algorithm

Modeling the Enantioselective Enzymatic Reaction with Modified Genetic Docking Algorithm

Validation of a two‐parameter quantitative structure–activity relationship as a legitimate tool for rational re‐design of horseradish peroxidase

Quantitative Structure−Activity Relationship Based Quantification of the Impacts of Enzyme−Substrate Binding on Rates of Peroxidase-Mediated Reactions of Estrogenic Phenolic Chemicals

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