Kinetic and molecular orbital studies on the rate of oxidation of monosubstituted phenols and anilines by lactoperoxidase compound II in comparison with the case of horseradish peroxidase |
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Authors: | Koichi Sato Toichiro Hosoya |
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Institution: | (1) Faculty of Pharmaceutical Sciences, Chiba University, 260 Chiba, Japan |
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Abstract: | The second-order rate constant (k4) for the oxidation of monosubstituted phenols and anilines by lactoperoxidase compound II was examined by Chance's method B. Chance, Arch. Biochem. Biophys.
71 (1957), 130–136]. When the electronic states of these substrates were calculated by an ab initio molecular orbital method, it was found that the log k4 value correlates well with the highest occupied molecular orbital (HOMO) energy level but not with the net charge or frontier electron density. These results are essentially similar to those reported previously in the case of horseradish peroxidase J. Sakurada, R. Sekiguchi, K. Sato, and T. Hosoya, Biochemistry
29 (1990), 4093–4098], showing some dissimilar features which are considered to reflect the structural difference between the two enzymes.Abbreviations HOMO
highest occupied molecular orbital
- HRP
horseradish peroxidase
- LPO
lactoperoxidase (EC 1.11.1.7)
- LUMO
lowest unoccupied molecular orbital |
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Keywords: | Lactoperoxidase phenols anilines HOMO energy Hammett's value" target="_blank">gif" alt="sgr" align="BASELINE" BORDER="0"> value ab initio molecular orbital method |
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