Formation of compound I of horseradish peroxidase in AOT reverse micelles as studied by pulse radiolysis and stopped-flow methods

1995 ◽  
Vol 98 (1) ◽  
pp. L1-L4 ◽  
Author(s):  
Lidia Gbicka ◽  
Jerzy L. Gbicki ◽  
Jarosław Pawlak
Keyword(s):  
Horseradish Peroxidase ◽  
Reverse Micelles ◽  
Pulse Radiolysis ◽  
Stopped Flow ◽  
Compound I ◽  
Aot Reverse Micelles

scholarly journals Intermicellar material exchange in reverse micelles formed by ionic AOT and nonionic Igepal surfactants studied by means of pulse radiolysis. Influence of the temperature

2004 ◽  
Vol 2 (2) ◽  
pp. 371-387 ◽  
Author(s):  
Jerzy Gębicki
Keyword(s):  
Reverse Micelles ◽  
Pulse Radiolysis ◽  
Nonionic Surfactants ◽  
Activation Enthalpy ◽  
Exchange Process ◽  
Activation Parameters ◽  
Aot Reverse Micelles ◽  
Droplet Concentration ◽  
Enthalpy And Entropy ◽  
Material Exchange

AbstractThe recombination of thiocyanate anion radicals, (SCN)2−, formed pulse radiolytically within the water pools of reverse micelles stabilized with anionic AOT and nonionic Igepal surfactants, was proved as an indicator reaction to study intermicellar exchange. It was found that the exchange process is slower inIgepal than in AOT reverse micelles with the same water to surfactant ratio. The apparent activation enthalpy and entropy of the exchange process were determined in different alkanes. For the AOT and Igepal reverse micelles the activation parameters increase with the droplet size, but for the AOT systems they do not significantly change with the increase of droplet concentration. For non-percolated systems the activation parameters for Igepal reverse micelles approach those for AOT reverse micelles. This result supports existing suggestions that the mechanism of intermicellar exchange does not differ in principle between reverse micelles stabilized with ionic and nonionic surfactants.

Horseradish Peroxidase. XVIII. The Arrhenius Activation Energy for the Formation of Compound I

1975 ◽  
Vol 53 (13) ◽  
pp. 1928-1932 ◽  
Author(s):  
W. D. Hewson ◽  
H. B. Dunford
Keyword(s):  
Activation Energy ◽  
Hydrogen Peroxide ◽  
Horseradish Peroxidase ◽  
Arrhenius Plot ◽  
Stopped Flow ◽  
Compound I ◽  
Arrhenius Activation Energy ◽  
Flow Apparatus ◽  
Absorbance Changes ◽  
Native Horseradish Peroxidase

The rate of formation of compound I from the reaction of native horseradish peroxidase with hydrogen peroxide was studied from 3.7–70.0 °C. The second-order rate constants were used to construct an Arrhenius plot from which the activation energy of this reaction was calculated to be 3.5 ± 1.0 kcal/mol. The irreversibility of the reaction at 25 °C was confirmed by comparing absolute absorbance changes as recorded by the stopped-flow apparatus with the known spectra of the native enzyme and compound I.

Study of peroxidase mechanisms by pulse radiolysis. II. Reaction of horseradish peroxidase Compound I with O2−

1974 ◽  
Vol 350 (1) ◽  
pp. 113-120 ◽  
Author(s):  
Benon H.J. Bielski ◽  
David A. Comstock ◽  
Arthur Haber ◽  
Phillip C. Chan
Keyword(s):  
Horseradish Peroxidase ◽  
Pulse Radiolysis ◽  
Compound I
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