Oxidation of phenols by horseradish peroxidase and lactoperoxidase compound II--kinetic considerations.
Oxidation of para substituted phenols by horseradish peroxidase compound II (HRP-II) and lactoperoxidase compound II (LPO-II) were studied using stopped flow technique. Apparent second order rate constants (kapp) of the reactions were determined. The kinetics of oxidation of phenols by HRP-II and LPO-II have been compared with the oxidation potentials of the substrates. Reorganization energies of electron-transfer of phenols to the enzymes were estimated from the variation of second order rate constants with the thermodynamic driving force.
Zahida
M S
MS
Department of Chemical Sciences, Tata Institute of Fundamental Research, Navy Nagar, Bombay.
Deva
W
W
Peerzada
G M
GM
Behere
D V
DV
D006735:Horseradish Peroxidase / Q000378:metabolism*; D007700:Kinetics; D007784:Lactoperoxidase / Q000378:metabolism*; D010084:Oxidation-Reduction; D010636:Phenols / Q000737:chemistry / Q000378:metabolism*
D010636:Phenols; D006735:Horseradish Peroxidase; D007784:Lactoperoxidase