Differential substrate behaviour of phenol and aniline derivatives during oxidation by horseradish peroxidase: kinetic evidence for a two-step mechanism

Gilabert, Marı́a Angeles

doi:10.1016/s1570-9639(04)00067-6

Cited by 23 publications

(3 citation statements)

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“…1-3 in Chart 1). 15,16) Since the oxidation of rifampicin matches these criteria, we used this model to determine the turnover number (k cat ) for its oxidation.…”

Section: Resultsmentioning

confidence: 99%

Horseradish Peroxidase-Catalyzed Oxidation of Rifampicin: Reaction Rate Enhancement by Co-oxidation with Anti-inflammatory Drugs

Santos

Ximenes

Fonseca

et al. 2005

Biological & Pharmaceutical Bulletin

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“…1-3 in Chart 1). 15,16) Since the oxidation of rifampicin matches these criteria, we used this model to determine the turnover number (k cat ) for its oxidation.…”

Section: Resultsmentioning

confidence: 99%

Horseradish Peroxidase-Catalyzed Oxidation of Rifampicin: Reaction Rate Enhancement by Co-oxidation with Anti-inflammatory Drugs

Santos

Ximenes

Fonseca

et al. 2005

Biological & Pharmaceutical Bulletin

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“…Despite early work by Bordeleau et al 1972 indicating a correlation between compound II reactivity and atomic charge on the substrate's phenolic oxygen, Hosoya et al 1983 andSakurada et al 1990 were unable to confirm significant correlation. Job et al 1976, Dunford et al 1986, Sakurada et al 1990, and Gilabert et al 2004 proteins in which the active pocket was opened, and they determined that HRP reactivity (i.e. k cat ) was reasonably correlated (R 2 = 0.81) with predicted binding distances.…”

Section: Kinetics Determining Factorsmentioning

confidence: 99%

Chemical kinetics and interactions involved in horseradish peroxidase-mediated oxidative polymerization of phenolic compounds

Cheng

Harper

2012

Enzyme and Microbial Technology

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iv To address the growing need for removing the emerging endocrine disrupting compounds (EDCs), the enzyme-based oxidative coupling reaction is suggested as promising alternative in consideration of its generally high specificity and removal efficiency on treatment of waters containing estrogenic phenolic chemicals.Various factors that affect the reaction rate of oxidative coupling (OXC) reaction of phenolic estrogens catalyzed by Horseradish Peroxidase (HRP) were evaluated in this study. Kinetic parameters were obtained for the removal of phenol as well as natural and synthetic estrogens estrone (E 1 ), 17β-estradiol (E 2 ), estriol (E 3 ), and 17α-ethinylestradiol (EE 2 ). Molecular orbital theory and Autodock software were employed to analyze chemical properties and substrate binding characteristics. It is found that the reactions were first order with respect to phenolic concentration and reaction rate constants (k r ) were determined for phenol, E 3 , E 1 , E 2 and EE 2 (in increasing order). It is also found that oxidative coupling was controlled by enzyme-substrate interactions, not diffusion. Docking simulations show that higher binding energy and shorter binding distance both promote more favorable kinetics. This research is the first to show that the OXC of phenolics is an entropy-driven and enthalpy-retarded process.

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“…The kinetics indicated that a two-step mechanism operated, in which the first step corresponded to the formation of an enzyme-substrate complex, and the second step corresponded to the electron transfer from the substrate to the iron atom. The size and hydrophobicity of the substrates controlled their access to the hydrophobic binding site of HRPC [64][65][66]. In general, the electron donating substituents on the para-site resulted in higher values of reaction rate constants.…”

Section: The Substituent Positionmentioning

confidence: 99%

Enzymatic Catalysis in the Synthesis of Polyanilines and Derivatives of Polyanilines

Xu¹,

Singh

Kaplan³

Enzyme-Catalyzed Synthesis of Polymers

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Differential substrate behaviour of phenol and aniline derivatives during oxidation by horseradish peroxidase: kinetic evidence for a two-step mechanism

Cited by 23 publications

References 0 publications

Horseradish Peroxidase-Catalyzed Oxidation of Rifampicin: Reaction Rate Enhancement by Co-oxidation with Anti-inflammatory Drugs

Horseradish Peroxidase-Catalyzed Oxidation of Rifampicin: Reaction Rate Enhancement by Co-oxidation with Anti-inflammatory Drugs

Chemical kinetics and interactions involved in horseradish peroxidase-mediated oxidative polymerization of phenolic compounds

Enzymatic Catalysis in the Synthesis of Polyanilines and Derivatives of Polyanilines

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