ChemInform Abstract: Mechanism of Peroxidase Oxidation. Substrate-Substrate Activation in Horseradish Peroxidase-Catalyzed Reactions

ChemInform ◽  
2010 ◽  
Vol 27 (26) ◽  
pp. no-no
Author(s):  
O. V. LEBEDEVA ◽  
N. N. UGAROVA
Keyword(s):  
Horseradish Peroxidase ◽  
Substrate Activation ◽  
Catalyzed Reactions ◽  
Peroxidase Oxidation

Horseradish Peroxidase Oxidation of Tyrosine-Containing Peptides and Their Subsequent Polymerization:  A Kinetic Study†

Biochemistry ◽  
1997 ◽  
Vol 36 (28) ◽  
pp. 8504-8513 ◽  
Author(s):  
Thierry Michon ◽  
Michel Chenu ◽  
Nicolas Kellershon ◽  
Michel Desmadril ◽  
Jacques Guéguen
Keyword(s):  
Horseradish Peroxidase ◽  
Kinetic Study ◽  
Peroxidase Oxidation

scholarly journals HORSERADISH PEROXIDASE CATALYZED DEGRADATION OF BROMOPHENOL BLUE DYE

2020 ◽  
Vol 64 (1) ◽  
pp. 93-98
Author(s):  
Anna A. Solovyeva ◽  
Thi Trinh Pham ◽  
Olga E. Lebedeva ◽  
Maria N. Ustinova
Keyword(s):  
Hydrogen Peroxide ◽  
Horseradish Peroxidase ◽  
Dye Degradation ◽  
Enzymatic Reaction ◽  
Oxidative Degradation ◽  
Bromophenol Blue ◽  
Blue Dye ◽  
Time Interval ◽  
Bromophenol Blue Dye ◽  
Peroxidase Oxidation

In this study, the oxidative destruction of bromophenol blue dye with hydrogen peroxide was carried out at pH 4.0-4.1 in the presence of a commercial horseradish peroxidase, as well as peroxidase isolated directly from horseradish roots (Armoracia rusticana). To determine peroxidase activity, a model reaction of the oxidation of phenol to quinone was used. With a dye concentration of 32.7 μM, the optimal concentration of hydrogen peroxide was 0.04 mM at peroxidase concentration of 1.15 nM. The optimal temperature of the enzymatic reaction was determined: at 23 °С for 10 min 90% of the dye was exposed to destruction. When the temperature rises to 50 °С, the reaction rate decreases, and the degree of destruction is 56% for the same time interval. It was shown that the initial rate of peroxidase oxidation of bromophenol blue follows Michaelis-Menten equation. The kinetic parameters of the enzymatic reaction were determined by linearizing Michaelis-Menten equation in Lineweaver-Burk coordinates. It was found that for the peroxidase oxidation reaction of bromophenol blue Michaelis constant and maximum rate were 42.7 μM and 57.5 μM·min–1, respectively. In this work, а high percentage of dye degradation was also achieved when using peroxidase isolated from horseradish roots. The experiments were conducted at a temperature of 30оС and pH 4.1. With the increase in the volume of the extract from 0.1 to 0.2 ml, the percentage decolorization increases from 75% to 90%. The results demonstrate the high degradation efficiency of bromophenol blue with the participation of the commercial horseradish peroxidase and peroxidase isolated from horseradish roots. Enzymatic oxidative degradation can be considered as an alternative to biodegradation.

NAD+ Cofactor Regeneration by TMB-Mediated Horseradish-Peroxidase-Catalyzed Reactions

2018 ◽  
Vol 3 (39) ◽  
pp. 10900-10904 ◽  
Author(s):  
Yunzhe Li ◽  
Zhen-Gang Wang ◽  
Huanrong Li ◽  
Baoquan Ding
Keyword(s):  
Horseradish Peroxidase ◽  
Cofactor Regeneration ◽  
Catalyzed Reactions

scholarly journals Phenothiazines are slowly oxidizable substrates of horseradish peroxidase

2011 ◽  
Vol 57 (5) ◽  
pp. 544-553 ◽  
Author(s):  
T.V. Rogozhina ◽  
V.V. Rogozhin
Keyword(s):  
Steady State ◽  
Horseradish Peroxidase ◽  
Reaction Medium ◽  
Substrate Oxidation ◽  
Substrate Complex ◽  
Enzyme Substrate ◽  
Steady State Kinetic ◽  
State Kinetic ◽  
Full Conversion ◽  
Peroxidase Oxidation

Reactions of peroxidase oxidation of triftazine and thioproperazine have been investigated in the presence of horseradish peroxidase using steady state kinetic methods. It has been shown that phenothiazines are slowly oxidizable substrates for horseradish peroxidase. kcat and Km values have been determined in the range of pH from 4.5 to 7.5. The study of co-oxidation of phenothiazines and o-dianisidine (ODN) revealed that in the presence of aminazine and ODN in the reaction medium both substances follow sequential oxidation. ODN oxidation was not observed until full conversion of aminazine. At pH 4.5-5.5 thioproperazine bound to the enzyme-substrate complex and caused a nticompetitive inhibition of peroxidase. At pH>5.5 sequential substrate oxidation with preferential thioproperazine conversion occurred. In the range of pH from 4.5 to 7.5 triftazine did not influence ODN oxidation.

scholarly journals Scanning Electrochemical Impedance Microscopy in Redox-Competition Mode for the Investigation of Antibodies Labelled with Horseradish Peroxidase

Materials ◽  
2021 ◽  
Vol 14 (15) ◽  
pp. 4301
Author(s):  
Antanas Zinovicius ◽  
Inga Morkvenaite-Vilkonciene ◽  
Almira Ramanaviciene ◽  
Juste Rozene ◽  
Anton Popov ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Charge Transfer ◽  
Horseradish Peroxidase ◽  
Electrochemical Impedance ◽  
Electric Circuit ◽  
Charge Transfer Resistance ◽  
Transfer Resistance ◽  
Immobilized Antibodies ◽  
Solution Resistance ◽  
Catalyzed Reactions

Scanning electrochemical microscopy enhanced by electrochemical impedance spectroscopy (SEIM) was applied to detect immobilized antibodies labelled with horseradish peroxidase (Ab-HRP). The localized HRP activity was investigated by the SEIM redox competition (RC-SEIM) mode using hydrogen peroxide as a substrate and hexacyanoferrate as a redox mediator. Electrochemical impedance shows to be related to the consumption of hydrogen peroxide at the ultramicroelectrode. For the evaluation of impedimetric results, an equivalent electric circuit was applied with solution resistance, double-layer capacitance, and charge-transfer resistance. These equivalent circuit characteristics depend on the distance between the sample and ultramicroelectrode, and the concentration of substrate. From the gathered data, the charge-transfer resistance appeared to be the parameter describing the behavior of HRP catalyzed reaction as it showed a linear dependence on H2O2 concentration. The RC-SEIM mode suitability for the studying of HRP catalyzed reactions and for the evaluation of Ab-HRP bound to the surface was demonstrated. Additionally, the applicability of RC-SEIM mode for the determination of Ab-HRP affinity bound to the target analyte was discussed.

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